Research
Aboytes Torres, R., Y. Liang, and Schulze T. I.
(1996). Analisis de la expresion in vitro del gene de la hemaglutinina del
virus de la influenza aviar via un marcador citoquimico y microscopia confocal
de rayo laser. [Analysis of the in vitro expression of the Ha gene from an
avian influenza virus, by using cytochemistry and confocal microscopy]. In:
Reunion Nacional de Investigacion Pecuaria, Cuernavaca, Morelos [Mexico], p.
49.
Abstract: El estudio fue disenado para
desarrollar un nuevo sistema de deteccion de la expresion in vitro de la
molecula de HA, utilizando como marcador citoquimico una fetoproteina y un
sistema de deteccion mediante microscopia confocal. El gene de la HA del virus
de la influenza aviar A/DW/WI/1938/80 (H1N1), fue insertado en el vector pREP10
y clonado en E. coli DH5 alfa. Monoestratos de celulas MDBK y MDCK con indices
de confluencia de entre 30 y 50% fueron transformados mediante la tecnica de
transfeccion con liposomas. La seleccion de celulas transformadas se llevo a
cabo con el tratamiento de los cultivos con higromicina como marcador de
seleccion (600 micro l/ml en medio DME completocon 10% v/v suero bovino fetal)
por un periodo de 3 a 4 semanas. Los cultivos celulares transformados en forma
estable fueron crecidos en cubreobjetos y fijados en paraformaldehido (3.7% en
PBS pH 7.2). La expresion temporal o constitutiva del gene de la HA en celulas
mamiferas transformadas fue monitoreada con las tecnicas estandarizadas de IFI
(con anticuerpos mono y policlonales), hemoadsorcion y hemoaglutinacion. La
nueva tecnica alternativa desarrollada se baso en la reaccion de acoplamiento
mediada por la alta afinidad entre el sitio de reconocimiento del recptor,
situado en los polipeptidos de la molecula de HA y el acido sialico de la
fetoproteina bovina (0.2% acido acetilneuroamidico) conjugada con oro coloidal
(10nm). Los ensayos incluyeron los analisis de la reaccion a nivel de
citoplasma y de superficie. Para este efecto se utilizaron monoestratos
permeabilizados con el detergente Tween 20 (0.05%) y monoestratos no
permeabilizadas. Los controles incluyeron celulas infectadas con virus
homologos y heterologos (WSN). Se concluye que la nueva tecnica descrita,
ofrece una alta especificidad y sensibilidad analitica en la deteccion de HA
expresada in vitro a la vez que es rapida y sencilla. Ademas, el potencial de
esta tecnica puede ser extrapolado en ensayos utilizando microscopia optica.
Descriptors: avian influenza virus,
cytochemistry, cell structure, confocal microscopy, influenza virus, viruses.
Air, G.M., L.R. Ritchie, W.G. Laver, and P.M. Colman
(1985). Gene and protein sequence of an influenza neuraminidase with
hemagglutinin activity. Virology 145(1): 117-22. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: An influenza virus neuraminidase (NA) of the
N9 subtype also has hemagglutinin (HA) activity (W. G. Laver, P. M. Colman, R.
G. Webster, V. S. Hinshaw, and G. M. Air (1984), Virology 137, 314-323). To
determine sequence relationships between this NA and other known NA and HA
subtype sequences, and as a necessary step toward a complete structure
determination, we have cloned a full-length copy of the coding sequence of the
N9 NA of influenza virus A/tern/Australia/G70C/75 into the plasmid pUC9 using
SalI linkers. The gene was sequenced by directed subcloning into the
single-stranded phage vectors M13mp19 and M13mp18 and use of the dideoxy
procedure. Most of the NA sequence was also obtained by direct protein
sequencing of tryptic peptides. The N9 NA has 43 and 44% homology when compared
to N1 or N2 sequences, respectively. There is no significant homology to any
known HA sequence, or to the HN protein of the paramyxovirus SV5. Like the
other NA molecules, the N9 NA is anchored in the membrane by an N-terminal
hydrophobic region, from which biologically active heads can be released by
pronase.
Descriptors: genes viral, hemagglutinins viral, influenza
A virus avian enzymology, influenza A virus enzymology, neuraminidase genetics,
amino acid sequence, base sequence, cloning, molecular, influenza A virus avian
genetics, avian immunology, influenza A virus genetics, influenza A virus
immunology.
Akhmatullina, N.B. and K.G. Mustafin (1982). Biologicheski
aktivnye ribonukleoproteidy kletok, zarazhennykh virusom chumy ptits.
[Biologically active ribonucleoproteins of cells infected with fowl plague
virus]. Voprosy Virusologii (1): 29-32. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The results of studies of physico-chemical
and biological properties of virus-specific ribonucleoproteins (RNP) in
influenza infection are presented. Particular attention is given to the
infectious properties of RNP. The earliest infectivity was found to be
associated with RNP structures sedimenting from nuclear extract in a zone of
30-40S.
Descriptors: nucleoproteins pharmacology,
ribonucleoproteins pharmacology, cell nucleus microbiology, chemistry,
physical, chick embryo, cytoplasm microbiology, influenza A virus avian
pathogenicity, ribonucleoproteins isolation and purification, species
specificity, time factors, virus cultivation.
Akkina, R.K. (1990). Antigenic reactivity and
electrophoretic migrational heterogeneity of the three polymerase proteins of
type A human and animal influenza viruses. Archives of Virology
111(3-4): 187-97. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Antigenic reactivity of the three polymerase
proteins PB1, PB2, and PA of type A influenza viruses of animal and human
origin were analysed by radioimmunoprecipitation using monospecific antisera.
Each of the polymerase monospecific antisera made against the polymerase
proteins of the human A/WSN/33 (H1N1) influenza virus reacted efficiently with
the homologous proteins of all the known thirteen HA subtype viruses of avian
influenza virus, three subtypes of human influenza virus, swine and equine
influenza viruses. This broad reactivity of each of the antisera indicated that
the polymerase proteins are antigenically related among the type A influenza
viruses and therefore can be considered as type specific antigens similar to
the other viral internal proteins nucleoprotein (NP) and matrix protein (M). No
electrophoretic migrational heterogeneity was found among the PB2 proteins of
different subtype viruses, whereas PB1 protein exhibited minor variation.
However, PA protein from among various viral subtypes showed considerable
heterogeneity. Each of the polymerase antisera also immunoprecipitated
additional antigenically related polypeptides with distinct electrophoretic
mobilities from cells infected with each of the influenza viral subtypes.
Descriptors: DNA directed RNA polymerases immunology,
influenza A virus human enzymology, influenza A virus enzymology, viral
proteins immunology, antigens, viral immunology, human immunology, influenza A
virus immunology, precipitin tests.
Alexander, D.J., M.S. Collins, and M. Parkinson.
(1981). Plaque-forming ability in MDCK cells and structure of the
haemagglutinin of influenza A viruses which differ in virulence for chickens.
In: Proceedings of the First International Symposium on Avian Influenza,
Beltsville, Maryland, USA, p. 148-156.
NAL
Call Number:
aSF995.6.I6I5 1981a
Descriptors: avian influenza A virus, virulence,
hemagglutinin, cells, chickens.
Alexander, D.J., G. Parsons, and R.J. Manvell (1986).
Experimental assessment of the pathogenicity of eight avian influenza A
viruses of H5 subtype for chickens, turkeys, ducks and quail. Avian
Pathology 15(4): 647-662. ISSN:
0307-9457.
NAL
Call Number: SF995.A1A9
Descriptors: avian influenza virus, chickens,
turkeys, ducks, quails, chickens, immune
response, disease transmission, clinical signs, mortality.
Alexander, D.J., G.F. Wood, M.S. Collins, J. Banks,
and R.J. Manvell (1996). Recent work on the pathogenicity of avian influenza
viruses and the pathogenicity and antigenicity of Newcastle disease virus. Proceedings
of the Western Poultry Diseases Conference 45: 1-4.
NAL
Call Number: SF995.W4
Descriptors: Newcastle disease virus, avian influenza
virus, influenza virus, orthomyxoviridae, paramyxoviridae, viruses.
Almeida, J.D. and C.M. Brand (1975). A
morphological study of the internal component of influenza virus. Journal of General Virology 27(3):
313-8. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Rapid treatment of influenza virus directly
on the microscope grid with non-ionic detergent had allowed better
visualization of the internal component. Many micrographs show that this
ribonucleoprotein (RNP) is present as a continuous stand of 6 nm diam. arranged
in the form of a double coil or helix. In spite of the minimal treatment to
which the virus was subjected most helices still showed signs of degradation.
The findings that we have obtained lead us to suggest that the RNP component of
influenza virus must be very sensitive to both chemical and physical
manipulations, any of which could cause it to fracture from one continuous
strand into several pieces, although such breakages could possibly occur at
specific points along its length.
Descriptors: orthomyxoviridae ultrastructure, RNA, viral,
viral proteins, chick embryo, cyprinidae, influenza A virus avian
ultrastructure, microscopy, electron, phosphotungstic acid, recombination,
genetic, surface active agents, tissue culture.
Almeida, J.D. and A.P. Waterson (1967). Some
observations on the envelope of an influenza virus. Journal of General
Microbiology 46(1): 107-10. ISSN:
0022-1287.
NAL
Call Number: 448.3 J823
Descriptors: influenza A virus avian, lipoproteins
analysis, microscopy, electron, viral proteins analysis.
Almond, J.W. (1977). A single gene determines the
host range of influenza virus. Nature 270(5638): 617-8. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: genes viral, influenza A virus avian
genetics, virus replication, cell line, DNA directed RNA polymerases genetics,
DNA directed RNA polymerases metabolism, avian physiology, RNA viral genetics,
viral proteins genetics, viral proteins physiology.
Almond, J.W. and R.D. Barry (1979). Genetic
recombination between two strains of fowl plague virus: construction of genetic
maps. Virology 92(2): 407-15.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus avian
genetics, RNA viral genetics, electrophoresis, polyacrylamide gel, avian
analysis, viral analysis, recombination, genetic, viral proteins analysis,
viral proteins biosynthesis.
Almond, J.W. and V. Felsenreich (1982). Phosphorylation
of the nucleoprotein of an avian influenza virus. Journal of General
Virology 60(Pt. 2): 295-305. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: High resolution polyacrylamide gel
electrophoresis (PAGE) of chick embryo fibroblast cells infected with the avian
influenza virus FPV-Rostock revealed two distinct polypeptides migrating in the
region of the nucleoprotein (NP). One-dimensional fingerprinting of these
polypeptides showed that they were both nucleoprotein, and [32P]orthophosphate
labelling revealed that they differed with respect to their state of
phosphorylation. Pulse-chase studies using [35S]methionine indicated that
phosphorylation of a certain proportion of NP occurs rapidly after synthesis
and is associated with transport to the nucleus. Nucleoprotein which remained
in the cytoplasm was predominantly non-phosphorylated. Both the phosphorylated
and the non-phosphorylated types of NP were found in ribonucleoprotein
complexes (RNPs) of different densities isolated on renografin gradients, but
RNPs isolated from the nucleus contained much more phosphorylated NP than those
from the cytoplasm. The kinase responsible for nucleoprotein phosphorylation
appears to be influenced by temperature of incubation of the infected cells.
Descriptors: influenza A virus avian metabolism,
nucleoproteins metabolism, viral proteins metabolism, cell line, cell nucleus
analysis, cell nucleus metabolism, chick embryo, cytoplasm analysis,
fibroblasts, phosphorylation, protein kinases metabolism, ribonucleoproteins
analysis, temperature.
Almond, J.W., D. McGeoch, and R.D. Barry (1977). Method
for assigning temperature-sensitive mutations of influenza viruses to
individual segments of the genome. Virology 81(1): 62-73. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes, influenza A virus avian growth and development,
mutation, chick embryo, avian analysis, avian radiation effects, peptides
analysis, RNA viral analysis, recombination, genetic, temperature, tissue
culture, ultraviolet rays, viral proteins analysis, virus replication.
Almond, J.W., D. McGeoch, and R.D. Barry (1979). Temperature-sensitive
mutants of fowl plague virus: isolation and genetic characterization. Virology
92(2): 416-27. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: genes viral, influenza A virus avian
genetics, recombination, genetic, avian analysis, mutation, temperature, viral
proteins analysis, viral proteins biosynthesis.
Altmuller, A., W.M. Fitch, and C. Scholtissek (1989).
Biological and genetic evolution of the nucleoprotein gene of human
influenza A viruses. Journal of General Virology 70(Pt. 8): 2111-9.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: There is a significant difference in the
ability of human influenza A virus H1N1 strains isolated up to 1977 and those
isolated later to rescue temperature-sensitive mutants of fowl plague virus
with a defect in the nucleoprotein (NP) gene. Therefore the NP genes of five
human H1N1 and H3N2 influenza A virus strains, isolated between 1950 and 1978, have
been sequenced. By comparison with previous and more recent isolates, an
evolutionary pathway has been established. Three amino acid replacements were
found which might be responsible for the functional difference between the USSR
(1977) and the Brazil (1978) strains. The California (H1N1) strain isolated in
1978 had acquired by reassortment the NP gene of a human H3N2 virus circulating
at about 1977 as had been previously suggested by investigations involving
RNase fingerprint or hybridization techniques.
Descriptors: evolution, genes viral, influenza A virus
human genetics, nucleoproteins genetics, viral core proteins, viral proteins
genetics, amino acid sequence, base sequence, chick embryo, chickens, influenza
A virus avian genetics, molecular sequence data, mutation, sequence homology,
nucleic acid.
Altmuller, A., M. Kunerl, K. Muller, V.S. Hinshaw,
W.M. Fitch, and C. Scholtissek (1992). Genetic relatedness of the
nucleoprotein (NP) of recent swine, turkey, and human influenza A virus (H1N1)
isolates. Virus Research 22(1): 79-87. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The sequences of nucleoprotein (NP) genes of
recent human and turkey isolates of influenza A viruses, which serologically
could be correlated to contemporary swine viruses, were determined. These
sequences were closely related to the NPs of these swine viruses and they
formed a separate branch on the phylogenetic tree. While the early swine virus
from 1931 resembled the avian strains in consensus amino acids of the NP and in
its ability to rescue NP ts mutants of fowl plague virus in chicken embryo
cells, the later strains on that branch were different: at 15 positions they
have their own amino acids and they rescued the NP ts mutants only poorly. Of
the NPs of the human New Jersey/76 isolates analysed, one clustered with the
recent H1N1 swine viruses of the U.S.A., the other one with contemporary human
strains. Since the NP is one of the main determinants of species specificity it
is concluded that, although the H1N1 swine isolates from the U.S.A. form their
own branch in the phylogenetic tree, they can be transmitted to humans and
turkeys, but they do not spread further in these populations and so far have
not contributed to human pandemics. It is not very likely that they will do so
in future, since its branch in the phylogenetic tree develops further away from
the human and avian branch.
Descriptors: influenza A virus avian genetics, human
genetics, porcine genetics, nucleoproteins genetics, fowl plague microbiology,
influenza microbiology, phylogeny, sequence homology, nucleic acid, turkeys.
Anisimova, E., Y. Ghendon, and S. Markushin (1980). Ultrastructural
changes in cells induced by temperature-sensitive mutants of fowl plague virus
at permissive and non-permissive temperature. Journal of General
Virology 47(1): 11-8. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Ultrastructural changes developing in chick
embryo fibroblast cultures infected with a wild-type strain of fowl plague virus
(FPV) or one of six FPV temperature-sensitive (ts) mutants belonging to
different complementation groups were studied. Cells infected with wild-type
FPV and incubated at optimal (36 degrees C) or nonpermissive temperature (42
degrees C) displayed changes similar to those described for orthomyxoviruses.
The same patterns of changes were observed at 36 degrees C in cells infected
with ts mutants belonging to five of the complementation groups. Mutant ts 303,
possessing mutation-altered haemagglutinin, induced at 36 degrees C the
formation of virions carrying a considerably reduced number of spikes on their
surfaces. At 42 degrees C, cells infected with ts mutant 131, with a defective
primary transcription stage, showed no morphological changes and no formation
of electron-dense inclusions. Cells infected with ts mutants with defective
secondary transcription or replication displayed nuclear inclusions but no
formation of filamentous cytoplasmic structures or virions. Mutant ts 5 with
defective late morphogenesis induced formation of considerably enhanced numbers
of nuclear inclusions.
Descriptors: cell transformation, viral, influenza A virus
avian, cell nucleus ultrastructure, cultured cells, chick embryo, fibroblasts
ultrastructure, inclusion bodies, viral ultrastructure, microscopy, electron,
mutation, temperature, virion ultrastructure.
Anonymous (1998). From the Centers for Disease
Control and Prevention. Isolation of avian influenza A(H5N1) viruses from
humans--Hong Kong, May-December 1997. JAMA the Journal of the American
Medical Association 279(4): 263-4.
ISSN: 0098-7484.
NAL
Call Number: 448.9 Am37
Descriptors: influenza epidemiology, influenza A virus
avian isolation and purification, adolescent, adult, child, child, preschool,
Hong Kong epidemiology, influenza virology, middle aged.
Anonymous (1998). From the Centers for Disease
Control and Prevention. Update: isolation of avian influenza A(H5N1) viruses
from humans--Hong Kong, 1997-1998. JAMA the Journal of the American
Medical Association 279(5): 347-8.
ISSN: 0098-7484.
NAL
Call Number: 448.9 Am37
Descriptors: influenza epidemiology, influenza virology,
influenza A virus avian isolation and purification, Hong Kong epidemiology,
seroepidemiologic studies.
Anschutz, W., C. Scholtissek, and P. Rott (1972). Genetic
relationship between different influenza strains. Medical Microbiology
and Immunology 158(1): 26-31. ISSN:
0300-8584.
Descriptors: influenza strains, influenza A virus, genetic
relationships, Hong Kong.
Armstrong, S.J. and R.D. Barry (1974). The
topography of RNA synthesis in cells infected with fowl plague virus. Journal
of General Virology 24(3): 535-47.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian metabolism, RNA viral
biosynthesis, autoradiography, cell nucleus enzymology, cell nucleus
metabolism, cultured cells, chick
embryo, cytoplasm enzymology, DNA directed RNA polymerases metabolism,
deoxyadenosines pharmacology, fibroblasts, avian enzymology, avian growth and
development, mycotoxins pharmacology, Newcastle disease virus growth and
development, Newcastle disease virus metabolism, time factors, tritium, uracil
nucleotides metabolism, uridine metabolism,
virus replication.
Armstrong, S.J., M.C. Outlaw, and N.J. Dimmock (
1990). Morphological studies of the neutralization of influenza virus by
IgM. Journal of General Virology 71(Pt. 10): 2313-9.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Quantitative relationships between
neutralization, aggregation and attachment to monolayers of chick embryo
fibroblast (CEF) cells have been studied using a constant amount of influenza
A/fowl plague virus/Rostock/34 (H7N1) and varying amounts of purified mouse
polyclonal IgM directed against the haemagglutinin, the major viral
neutralization antigen. There are two major types of interaction. (i) At low
concentrations of IgM there is aggregation of virus, but no neutralization
provided that the aggregates are dispersed by vortexing and dilution. Maximum
aggregation occurs at less than seven molecules of IgM per virion and the IgM
is probably bound in the 'staple' or 'crab' conformation at these
concentrations. (ii) At higher concentrations there is neutralization and this
coincides with inhibition of attachment of virus to CEF cells. Neutralization
of 50% infectivity requires about 35 molecules of IgM per virion. The maximum
neutralization observed was only 87%. Quantitative data and electron microscopy
observations suggest that molecules of IgM at the higher concentrations adopt a
planar stance approximately perpendicular to the viral surface. It appears that
IgM neutralizes fowl plague virus in vitro primarily by interfering with its
attachment to cells; the fraction of neutralized virus that does attach is
known not be internalized.
Descriptors: antibodies, viral immunology, immunoglobulin
M immunology, influenza A virus avian immunology, antigen antibody complex,
immunohistochemistry, avian ultrastructure, microscopy, electron,
neutralization tests.
Asadullaev, T.A. and A.G. Bukrinskaia (1976). Kharakteristika
RNK, vydelennoi iz iadernogo RNK-sinteziruiushchego kompleksa virusa grippa.
[Characteristics of RNA isolated from the nuclear RNA-synthesizing complex of
influenza virus]. Voprosy Virusologii (6): 656-9. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: When Ehrlich ascitic carcinoma cells infected
with classical fowl plague virus and treated with actinomycin D were pulse
labeled for 10 min with 3H-uridine, it was mainly incorporated into nucleoplasm
structures sedimenting in sucrose gradients at 120S. At 2-hr exposure of the
infected cells to 3H-uridine radioactivity was found in nucleoplasm in the area
of 65S and in the cytoplasm in 30-40S zone. The analysis of RNA isolated from
these structures gave the following results. The RNA isolated from 120S
structures sedimented in two zones of sucrose gradient: 11S and 16-23S. The 11S
RNA was resistant to RNA-ase, while 16-23S RNA was sensitive to RNA-ase. A
similar (16-23S) RNA was isolated from virus-specific structures 65S and
30-40S.
Descriptors: influenza A virus avian, RNA viral
biosynthesis, viral isolation and purification, virus replication, carcinoma,
Ehrlich tumor analysis, carcinoma, Ehrlich tumor microbiology, catalysis, cell
nucleus metabolism, centrifugation, density gradient, ribonucleases,
transcription, genetic, uridine metabolism.
Asadullaev, T.A., A.K. Gitel'man, and A.G.
Bukrinskaia (1975). Abortivnaia infektsiia miksovirusov v kletkakh astsitnoi
kartsinomy Erlikha. Analiz virusspetsificheskikh struktur v astsitnoi
zhidkosti. [Abortive myxovirus infection of Ehrlich ascites carcinoma cells.
Analysis of virus-specific structures in the ascitic fluid]. Voprosy
Virusologii (3): 278-82. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Abstract: In the course of classical fowl plague virus
reproduction in Ehrlich ascites carcinoma cells both hemagglutinins and
S-antigen accumulate and titers of the infectious activity increase. However
virus reproduction does not terminate in formation of virus, and subviral
structures are found in the liquid fraction of the infected cells. Analysis of
these structures has shown them to have a sedimentation coefficient of 350-370S
and buovant density 1.29 g/ml. The rapidly sedimenting structure has
complement-fixing hemagglutinating activity but bow infectivity.
Descriptors: carcinoma, Ehrlich tumor microbiology,
influenza A virus avian growth and development, virus replication, amino acids,
antigens, viral analysis, carcinoma, Ehrlich tumor analysis, centrifugation,
density gradient, complement fixation tests, hemagglutinins viral analysis,
methionine, sulfur radioisotopes, tritium.
Assadullaeff, T., A.K. Gitelman, and A.G. Bukrinskaya
(1975). Influenza virus RNA-synthesizing complex in the nucleoplasm of
infected cells. Journal of General Virology 29(1): 137-42. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: An RNA-synthesizing complex was found in the
nucleoplasm of fowl plague virus-infected chicken fibroblast and Ehrlich tumour
cells. The complex sedimented at 120 S and banded in caesium chloride at 1-39
to 1-41 g/ml. It contained an influenza nucleocapsid protein as a major protein
constituent. The complex functioned late in infection, and RNA synthesis in it
was resistant to actinomycin D, the properties expected of influenza virus replicative
complex.
Descriptors: cell nucleus metabolism, influenza A virus
avian metabolism, RNA viral biosynthesis, carcinoma, Ehrlich tumor, chick
embryo, dactinomycin pharmacology, fibroblasts, avian growth and development,
mice, tissue culture, viral proteins biosynthesis, virus replication.
Astapovich, L.G., G.A. Ivanova, and S.B. Logginov
(1968). Elektronnomikroskopicheskoe izuchenie shtammov virusa klassicheskoi
chumy ptits. [An electron microscopic study of strains of the virus of classic
fowl plague]. Veterinariia 45(9): 24-6. ISSN: 0042-4846.
NAL
Call Number: 41.8 V6426
Descriptors: influenza A virus avian cytology, chick
embryo, microscopy, electron.
Atsev, S., I. Gagov, and I. Mikhailov (1981). Vurkhu
tsitologichite razlichiia v kletuchni kulturi, zarazeni s virusa na
klasicheskata chuma po ptitsite i gripen virus tip A. [Cytological differences
in cell cultures infected with classical fowl plague virus and influenza virus
type A]. Acta Microbiologica Bulgarica 9: 79-86. ISSN: 0204-8809.
NAL
Call Number: QR1.A37
Descriptors: influenza A virus avian pathogenicity,
cattle, cytopathogenic effect, viral, time factors, virus cultivation, virus
replication.
Austin, F.J., Y. Kawaoka, and R.G. Webster (1990). Molecular
analysis of the haemagglutinin gene of an avian H1N1 influenza virus. Journal
of General Virology 71(Pt. 10): 2471-4.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: This study presents the first nucleotide
sequence and deduced primary amino acid sequence of a subtype H1 haemagglutinin
from the avian influenza virus A/duck/Alberta/35/76 (H1N1). The molecule is
structurally, antigenically and molecularly similar to H1 haemagglutinins of
human viruses but sequence homology differences indicate that there has not
been a recent transfer of haemagglutinin genetic information between them.
Descriptors: hemagglutinins viral genetics, influenza A
virus avian genetics, amino acid sequence, base sequence, genes, structural,
viral, avian immunology, molecular sequence data.
Austin, F.J. and R.G. Webster (1986). Antigenic
mapping of an avian H1 influenza virus haemagglutinin and interrelationships of
H1 viruses from humans, pigs and birds. Journal of General Virology
67(Pt. 6): 983-92. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Monoclonal antibodies to the haemagglutinin
(HA) of the avian H1 influenza virus A/duck/Alberta/35/76 were used to
construct an operational antigenic map of the HA molecule and to study the
interrelationships of H1 viruses from different hosts. Haemagglutination
inhibition tests between the monoclonal antibodies and variants selected by
them provided evidence of four antigenic regions which overlap to varying
degrees. Avian H1 influenza viruses displayed a spectrum of reactivities to the
monoclonal antibody panel. Representatives of the epidemic strains of human H1
influenza viruses and early swine influenza viruses showed little or no
reactivity with the monoclonal antibodies but swine influenza-like viruses
isolated from pigs and humans in the last decade reacted with 11 of 17
antibodies. The antigenic similarity of these viruses to many avian isolates
suggests that there has been a transfer of HA genetic information between
mammalian and avian H1 influenza viruses.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, antibodies, monoclonal diagnostic use, epitopes, human
immunology, porcine immunology, species specificity.
Avery, R.J. (1975). Abortive infection of L cells
by influenza virus: absence of virion RNA synthesis. Journal of Virology
16(2): 311-4. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Influenza virus multiplies productively in
chick cells and abortively in L cells. The infecting influenza virus RNA
genomes are less stable in infected L cells than in infected chick cells.
However, transcription of the virus genome in L cells, while reduced in rate,
is not decreased in extent. There is no detectable synthesis of virion RNA in L
cells, and this is the most likely cause of the abortive infection.
Descriptors: influenza A virus avian metabolism, L cells
cell line, RNA viral biosynthesis, chick embryo, fibroblasts, avian growth and
development, mice, nucleic acid hybridization, phosphorus radioisotopes, tissue
culture, transcription, genetic, virus replication.
Avery, R.J. (1974). The subcellular localization
of virus-specific RNA in influenza virus-infected cells. Journal of
General Virology 24(1): 77-88. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: influenza A virus avian growth and
development, RNA viral analysis, virus replication, base sequence, cell nucleus
analysis, chick embryo, cytoplasm analysis, nucleic acid hybridization, RNA,
ribosomal analysis, ribonucleases, time factors, tritium, uridine.
Aymard, M., A.R. Douglas, M. Fontaine, J.M. Gourreau,
C. Kaiser, J. Million, and J.J. Skehel (1985). Antigenic characterization of
influenza A (H1N1) viruses recently isolated from pigs and turkeys in France.
Bulletin of the World Health Organization 63(3): 537-42. ISSN: 0042-9686.
NAL
Call Number: 449.9 W892B
Descriptors: antigens, viral analysis, influenza A virus
avian immunology, porcine immunology, immunology, swine microbiology, turkeys
microbiology, France, avian isolation and purification, porcine isolation and
purification.
Baez, M., R. Taussig, J.J. Zazra, J.F. Young, P.
Palese, A. Reisfeld, and A.M. Skalka (1980). Complete nucleotide sequence of
the influenza A/PR/8/34 virus NS gene and comparison with the NS genes of the
A/Udorn/72 and A/FPV/Rostock/34 strains. Nucleic Acids Research
8(23): 5845-58. ISSN: 0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: The nucleotide sequence of the NS gene of the
human influenza virus A/PR/8/34 was determined and found to be the same length
(890 nucleotides) as the NS gene of another human influenza virus A/Udorn/72
and of the avian isolate A/FPV/Rostock/34. Comparison of the sequences of the
NS genes of the two human influenza viruses shows an 8.9% difference whereas the
NS gene of the avian isolate differs by only 8% from that of the human strain
A/PR/8/34. The extensive sequence similarity among these three genes does not
support the notion of species specific homology groups among NS genes of avian
and human influenza virus strains. The primary sequence of the A/PR/8/34 NS
gene is consistent with the findings that the influenza virus NS gene may code
for two overlapping polypeptides. In addition, an open reading frame
potentially coding for a polypeptide 167 amino acids in length was found in the
negative strand RNA of the A/PR/8/34 virus NS gene.
Descriptors: genes viral, influenza A virus avian
genetics, human genetics, RNA viral genetics, amino acid sequence, base
sequence, cloning, molecular, peptides genetics, species specificity.
Baigent, S.J., R.C. Bethell, and J.W. McCauley (
1999). Genetic analysis reveals that both haemagglutinin and neuraminidase
determine the sensitivity of naturally occurring avian influenza viruses to
zanamivir in vitro. Virology 263(2): 323-38. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: antiviral agents pharmacology, genes viral
physiology, hemagglutinins viral metabolism, influenza A virus avian drug
effects, neuraminidase antagonists and inhibitors, neuraminidase metabolism,
sialic acids pharmacology, amino acid sequence, base sequence, cultured cells,
chick embryo, chickens blood, chickens virology, dogs, erythrocytes virology,
genes viral genetics, glycosylation,
hemagglutination, viral drug effects, hemagglutinins viral genetics,
avian enzymology, avian genetics, avian physiology, inhibitory concentration
50, lactose analogs and derivatives, lactose metabolism, molecular sequence
data, mutation genetics, neuraminidase chemistry, neuraminidase genetics,
reassortant viruses drug effects, reassortant viruses enzymology, reassortant
viruses genetics, reassortant viruses physiology, sialic acids metabolism,
substrate specificity, virus replication, drug effects.
Baigent, S.J. and J.W. McCauley (2001). Glycosylation
of haemagglutinin and stalk-length of neuraminidase combine to regulate the
growth of avian influenza viruses in tissue culture. Virus Research
79(1-2): 177-85. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: The influence on virus replication in culture
of the presence and location of glycosylation sites on the haemagglutinin (HA)
glycoprotein of avian influenza viruses and differences in length of the stalk
region of their neuraminidase (NA) glycoprotein was examined using reassortant
viruses. Plaque size was measured in the presence or absence of bacterial
neuraminidase (CPNA) and/or an influenza virus NA inhibitor, zanamivir, to
assess the relative contribution of the NA to replication efficiency in tissue
culture. The following conclusions were drawn, (1) HA lacking glycosylation at
158 gives inefficient growth when combined with short-stalked NAs, and
efficient growth when combined with long-stalked NAs. (2) Glycosylation at 158
of HA makes the virus less dependent on NA for release from its receptors. (3)
HA with glycosylation at 158 gives efficient growth when combined with
short-stalked NAs but, when combined with long-stalked NAs, growth is very
efficient and excess NA activity is disadvantageous. (4) HA having
glycosylation at 158 combined with short-stalked NAs, or HA lacking
glycosylation at 158 combined with long-stalked NAs may represent optimal
combinations. The results reinforce the importance of a balance of HA and NA
activity for efficient virus exit from, and entry into cells.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, influenza A virus avian growth and development, neuraminidase
metabolism, antiviral agents pharmacology, chick embryo, C lostridium
perfringens enzymology, enzyme inhibitors pharmacology, glycosylation,
hemagglutinin glycoproteins, influenza virus chemistry, hemagglutinin
glycoproteins, influenza virus genetics, avian drug effects, avian genetics,
avian physiology, neuraminidase antagonists and inhibitors, plaque assay,
protein structure, tertiary, sialic acids pharmacology.
Baker, A.T., J.N. Varghese, W.G. Laver, G.M. Air, and
P.M. Colman (1987). Three-dimensional structure of neuraminidase of subtype
N9 from an avian influenza virus. Proteins 2(2): 111-7. ISSN: 0887-3585.
NAL
Call Number: QP551.P698
Abstract: Neuraminidases from different subtypes of
influenza virus are characterized by the absence of serological
cross-reactivity and an amino acid sequence homology of approximately 50%. The
three-dimensional structure of the neuraminidase antigen of subtype N9 from an
avian influenza virus (A/tern/Australia/G70c/75) has been determined by X-ray
crystallography and shown to be folded similarly to neuraminidase of subtype N2
isolated from a human influenza virus. This result demonstrates that absence of
immunological cross-reactivity is no measure of dissimilarity of polypeptide
chain folding. Small differences in the way in which the subunits are organized
around the molecular fourfold axis are observed. Insertions and deletions with
respect to subtype N2 neuraminidase occur in four regions, only one of which is
located within the major antigenic determinants around the enzyme active site.
Descriptors: influenza A virus avian enzymology,
neuraminidase immunology, neuraminidase metabolism, amino acid sequence,
antigens, viral, binding sites, avian classification, models, molecular,
molecular sequence data, n acetylneuraminic acid, protein conformation, sialic
acids metabolism.
Banbura, M.W., Y. Kawaoka, T.L. Thomas, and R.G.
Webster (1991). Reassortants with equine 1 (H7N7) influenza virus
hemagglutinin in an avian influenza virus genetic background are pathogenic in
chickens. Virology 184(1): 469-471.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Reassortants possessing the hemagglutinin
(HA) gene from A/Equine/London/1416/73 (H7N7) [Eq/Lond) and five or more genes
from A/Chicken/Pennsylvania/1370/83 (H5N2) [Ck/Penn] were lethal in chickens.
This result demonstrates that horses can maintain influenza viruses whose HAs
are capable of promoting virulence. Thus, reassortment of equine and avian
influenza virus genes could generate viruses that might be lethal in domestic
poultry.
Descriptors: fowls, horses, avian influenza virus, equine
influenza virus, hemagglutinins, genes, amino acids, virulence, pathogenicity,
mortality, molecular sequence data, EMBL m58657, GENBANK m58657.
Bankowski, R.A. (1975). Interferon and its role in
poultry health. American Journal of Veterinary Research 36(4):
494-497. ISSN: 0002-9645.
NAL
Call Number: 41.8 Am3A
Descriptors: interferon, viral diseases, poultry.
Banks, J., E.C. Speidel, J.W. McCauley, and D.J.
Alexander (2000). Phylogenetic analysis of H7 haemagglutinin subtype
influenza A viruses. Archives of Virology 145(5): 1047-58. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: A 945 nucleotide region (bases 76-1020) of
the HA1 part of the HA gene was obtained for 31 influenza viruses of H7 subtype
isolated primarily from Europe, Asia and Australia over the last 20 years.
These were analysed phylogenetically and compared with sequences of the same
region from 23 H7 subtype viruses available in Genbank. The overall results
showed two geographically distinct lineages of North American and Eurasian
viruses with major sublineages of Australian, historical European and equine
viruses. Genetically related sublineages and clades within these major groups
appeared to reflect geographical and temporal parameters rather than being
defined by host avian species. Viruses of high and low virulence shared the
same phylogenetic branches, supporting the theory that virulent viruses are not
maintained as a separate entity in waterfowl.
Descriptors: hemagglutinin glycoproteins, influenza virus
genetics, influenza A virus avian classification, avian genetics, amino acid
sequence, fowl plague virology, genes viral, avian isolation and purification,
phylogeny, poultry, sequence homology, amino acid.
Banks, J., E.S. Speidel, E. Moore, L. Plowright, A.
Piccirillo, I. Capua, P. Cordioli, A. Fioretti, and D.J. Alexander (2001). Changes
in the haemagglutinin and the neuraminidase genes prior to the emergence of
highly pathogenic H7N1 avian influenza viruses in Italy. Archives of
Virology 146(5): 963-73. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Outbreaks of avian influenza due to an H7N1
virus of low pathogenicity occurred in domestic poultry in northern Italy from
March 1999 until December 1999 when a highly pathogenic avian influenza (HPAI)
virus emerged. Nucleotide sequences were determined for the HA1 and the stalk
region of the neuraminidase (NA) for viruses from the outbreaks. The HPAI
viruses have an unusual multibasic haemagglutinin (HA) cleavage site motif,
PEIPKGSRVRRGLF. Phylogenetic analysis showed that the HPAI viruses arose from low
pathogenicity viruses and that they are most closely related to a wild bird
isolate, A/teal/Taiwan/98. Additional glycosylation sites were present at amino
acid position 149 of the HA for two separate lineages, and at position 123 for
all HPAI and some low pathogenicity viruses. Other viruses had no additional
glycosylation sites. All viruses examined from the Italian outbreaks had a 22
amino acid deletion in the NA stalk that is not present in the N1 genes of the
wild bird viruses examined. We conclude that the Italian HPAI viruses arose
from low pathogenicity strains, and that a deletion in the NA stalk followed by
the acquisition of additional glycosylation near the receptor binding site of
HA1 may be an adaptation of H7 viruses to a new host species i.e. domestic
poultry.
Descriptors: fowl plague virology, hemagglutinins viral
genetics, influenza A virus avian genetics, neuraminidase genetics, poultry
diseases virology, amino acid motifs, amino acid sequence, birds virology,
chickens virology, disease outbreaks, evolution, molecular, fowl plague
epidemiology, genes, structural, viral, glycosylation, influenza A virus avian
isolation and purification, influenza A virus avian pathogenicity, Italy
epidemiology, molecular sequence data, phylogeny, poultry diseases
epidemiology, protein processing, post translational, sequence deletion,
sequence homology, turkeys virology, virulence genetics.
Bano, S., K. Naeem, and S.A. Malik (2003). Evaluation
of pathogenic potential of avian influenza virus serotype H9N2 in chickens.
Avian Diseases 47(Special Issue): 817-822. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Recently seven isolates of avian influenza
virus (AIV) serotype H9N2 recovered from an outbreak of AI were analyzed on the
basis of their biological and molecular characteristics. All the isolates
belonged to the low-pathogenicity group of AIV. To further evaluate their
pathogenic potential in association with other organisms, an isolate was
inoculated experimentally in chickens using different routes and subsequently
challenged with infectious bronchitis virus, Ornithobacterium rhinotracheale
or Escherichia coli. The virus isolation and seromonitoring data
revealed a significant role of Escherichia coli in aggravating the
clinical condition of the birds earlier infected with AIV (H9N2). The
AIV-antigen was detected in lung, trachea, kidney, and cloacal bursa among the
infected birds, using immunofluorescent antibody technique. In another
experiment, chickens that were immunosuppressed chemically showed high
mortality when challenged with AIV H9N2. The results indicated that this low
pathogenicity AIV (H9N2) isolate could produce severe infection depending on
the type of secondary opportunistic pathogens present under field conditions.
This may explain the severity of infection with the present H9N2 outbreak in
the field. A prolonged antibacterial therapy in flocks infected with AIV H9N2
and use of oil-based vaccine at an early age in new flocks has helped to control
this infection and the disease.
Descriptors: epidemiology, infection, avian influenza,
infectious disease, respiratory system disease, viral disease,
immunofluorescence, immunologic techniques, laboratory techniques, viral
isolation, disease outbreak, secondary opportunistic pathogens, seromonitoring
data.
Barich, N.L., E.A. Evteeva, and N.V. Kaverin (1992). Svoistva
vnutrikletochnykh virus-spetsificheskikh ribonukleoproteidov, soderzhashchikh
negativnye i pozitivnye RNK virusagrippa A. [Properties of intracellular
virus-specific ribonucleoproteins containing negative and positive hepatitis A
virus RNA]. Molekuliarnaia Genetika, Mikrobiologiia i Virusologiia
(9-10): 15-9. ISSN: 0208-0613.
NAL
Call Number: QH506.M65F2
Abstract: The characteristics of the intracellular
virus-specific nucleocapsids containing either a negative or a positive RNA
strand were studied. The immunosorption of nucleocapsids by the monoclonal
antibodies against the three epitopes of NP protein failed to reveal any
antigenic difference between the negative strand or positive strand-containing
nucleocapsids. On the other hand, the sensitivity of virus-specific RNA in the
nucleocapsids to digestion by the pancreatic ribonuclease proved to be lower
for the positive strand-containing nucleocapsids.
Descriptors: influenza A virus avian genetics, RNA viral
chemistry, ribonucleoproteins analysis, chick embryo, epitopes immunology,
ribonucleoproteins immunology.
Barry, R.D. and P. Davies (1970). The effects of
UK2054 on the multiplication of influenza viruses. Journal of Hygiene
68(1): 151-8. ISSN: 0022-1724.
NAL
Call Number: 449.8 J82
Descriptors: isoquinolines pharmacology, orthomyxoviridae
drug effects, chick embryo, fetal membranes, hemagglutination tests, immune
sera, influenza A virus avian drug effects, orthomyxoviridae growth and
development, virus inhibitors pharmacology.
Basak, S. and R.W. Compans (1983). Studies on the
role of glycosylation in the functions and antigenic properties of influenza
virus glycoproteins. Virology 128(1): 77-91. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The biological and antigenic roles of
glycosylation were investigated in the influenza hemagglutinin (HA)
glycoprotein using the glycosylation inhibitor tunicamycin (TM). Under conditions
where only the nonglycosylated form of HA was detected by immunoprecipitation
and gel electrophoresis, the migration of glycoproteins to the cell surface was
observed by immunofluorescence using either monospecific or monoclonal antibody
to the HA polypeptide. Analysis of the surface fluorescence in TM-treated
infected cells by a fluorescence-activated cell sorter (FACS) showed that all
cells exhibited fluorescence in the complete absence of glycosylation. The
relative amount of HA antigen on cell surfaces was found to be reduced by only
30-40% in TM-treated cells, and this reflected a similar reduction in
intracellular synthesis. Electron microscopic studies using ferritin labeling
also demonstrated that the nonglycosylated HA glycoprotein was present in
significant amounts on surfaces of infected cells. Virions with nonglycosylated
glycoproteins were purified, and were found to have an approximate 30-fold
decrease in both hemagglutinin and neuraminidase specific activities. The
possible role of oligosaccharides in antigenic variation among various H1N1
strains was investigated. Immunoprecipitation reactions involving five
different monoclonal antibodies and five antigenic variants of A/USSR/90/77
revealed no major antigenic differences between the glycosylated and
nonglycosylated forms of HA.
Descriptors: cell membrane analysis, hemagglutinins viral
analysis, influenza A virus avian analysis, human analysis, antibodies,
monoclonal immunology, antibodies, viral immunology, epitopes immunology, hemagglutination,
viral, hemagglutinin glycoproteins, influenza virus, hemagglutinins viral
immunology, neuraminidase metabolism, tunicamycin pharmacology.
Bashiruddin, J.B., A.R. Gould, and H.A. Westbury
(1992). Molecular pathotyping of two avian influenza viruses isolated during
the Victoria 1976 outbreak. Australian Veterinary Journal 69(6):
140-2. ISSN: 0005-0423.
NAL
Call Number: 41.8 Au72
Descriptors: chickens, disease outbreaks veterinary, fowl
plague microbiology, influenza A virus avian classification, RNA viral
analysis, amino acid sequence, base sequence, DNA, viral chemistry, fowl plague
epidemiology, hemagglutinins viral chemistry, hemagglutinins viral genetics,
influenza A virus avian genetics, molecular sequence data, polymerase chain
reaction, viral chemistry, Victoria epidemiology.
Baum, L.G. and J.C. Paulson (1990). Sialyloligosaccharides
of the respiratory epithelium in the selection of human influenza virus
receptor specificity. Acta Histochemica. Supplement Band 40:
35-8. ISSN: 0567-7556.
NAL
Call Number: 384 AC8
Abstract: Human H3 strains of influenza A virus
preferentially bind cell-surface oligosaccharides containing the sequence NeuAc
alpha 2,6Gal, while avian influenza strains preferentially recognize the
sequence NeuAc alpha 2,3Gal. The distribution of these two types of sialic acid
linkages on host respiratory epithelium, the target of influenza infection, may
be a factor in the selection of the different receptor specificities observed
in human and avian influenza strains. To examine the distribution of these two
structures on human tracheal epithelial cells, two sialic acid specific lectins
were used. The Sambucus nigra lectin (SNA), which recognizes the sequence NeuAc
alpha 2,6Gal/GalNac, primarily binds to the surface of the ciliated tracheal
epithelial cells, and only weakly binds to mucins in the surface goblet cells.
In contrast, the Maackia amurensis lectin (MAL), which is specific for the
NeuAc alpha 2,3Gal sequence, binds strongly to mucus droplets in goblet cells,
but not to the surface of ciliated cells. Thus, human ciliated tracheal cells
appear to contain sialyloligosaccharides preferentially recognized by human
influenza strains. These findings suggest that human H3 influenza strains may
have evolved a receptor specificity which favors binding to ciliated cells, and
minimizes binding inhibition by respiratory mucus.
Descriptors: influenza A virus human metabolism,
oligosaccharides metabolism, receptors, virus metabolism, trachea
ultrastructure, epithelial cells, epithelium metabolism, epithelium
ultrastructure, fluorescent antibody technique, fluorescent dyes diagnostic
use, histocytochemistry, protein binding, receptors, virus ultrastructure,
trachea cytology, trachea metabolism.
Bean, W.J. (1984). Correlation of influenza A
virus nucleoprotein genes with host species. Virology 133(2):
438-42. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The RNAs coding for the nucleoproteins of a
panel of influenza isolates from human and nonhuman hosts were compared by
RNA-RNA hybridization to determine the extent of genetic diversity of this
protein and to determine if related nucleoproteins (NP) are consistently found
in viruses from certain hosts. Five nucleoprotein groups were defined. Group 1
contains nearly all of the avian influenza viruses, group 2 includes only
certain viruses isolated from gulls, group 3 includes all recent equine
influenza strains, group 4 contains only equine/Prague/1/56, and group 5
contains all human and swine influenza isolates. The maintenance of specific
nucleoproteins in viruses from certain species suggests that these proteins
have evolved functionally significant differences that favor their replication
in a specific host.
Descriptors: cell transformation, viral, genes,
structural, genes viral, influenza A virus genetics, nucleoproteins genetics,
human genetics, porcine genetics, nucleic acid hybridization, RNA viral
genetics, species specificity.
Bean, W.J., Y. Kawaoka, J.M. Wood, J.E. Pearson, and
R.G. Webster (1985). Characterization of virulent and avirulent
A/chicken/Pennsylvania/83 influenza A viruses: potential role of defective
interfering RNAs in nature. Journal of Virology 54(1): 151-60. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: In April 1983, an influenza virus of low
virulence appeared in chickens in Pennsylvania. Subsequently, in October 1983,
the virus became virulent and caused high mortality in poultry. The causative
agent has been identified as an influenza virus of the H5N2 serotype. The
hemagglutinin is antigenically closely related to tern/South Africa/61 (H5N3)
and the neuraminidase is similar to that from human H2N2 strains (e.g.,
A/Japan/305/57) and from some avian influenza virus strains (e.g.,
A/turkey/Mass/66 [H6N2]). Comparison of the genome RNAs of chicken/Penn with
other influenza virus isolates by RNA-RNA hybridization indicated that all of
the genes of this virus were closely related to those of various other
influenza virus isolates from wild birds. Chickens infected with the virulent
strain shed high concentrations of virus in their feces (10(7) 50% egg
infective dose per g), and the virus was isolated from the albumin and yolk of
eggs layed just before death. Virus was also isolated from house flies in
chicken houses. Serological and virological studies showed that humans are not
susceptible to infection with the virus, but can serve as short-term mechanical
carriers. Analysis of the RNA of the viruses isolated in April and October by
gel migration and RNA-RNA hybridization suggested that these strains were very
closely related. Oligonucleotide mapping of the individual genes of virulent
and avirulent strains showed a limited number of changes in the genome RNAs,
but no consistent differences between the virulent and avirulent strains that could
be correlated with pathogenicity were found. Polyacrylamide gel analysis of the
early (avirulent) isolates demonstrated the presence of low-molecular-weight
RNA bands which is indicative of defective-interfering particles. These RNAs
were not present in the virulent isolates. Experimental infection of chickens
with mixtures of the avirulent and virulent strains demonstrated that the
avirulent virus interferes with the pathogenicity of the virulent virus. The
results suggest that the original avirulent virus was probably derived from
influenza viruses from wild birds and that the virulent strain was derived from
the avirulent strain by selective adaptation rather than by recombination or
the introduction of a new virus into the population. This adaptation may have
involved the loss of defective RNAs, as well as mutations, and thus provides a
possible model for a role of defective-interfering particles in nature.
Descriptors: chickens microbiology, influenza A virus
avian pathogenicity, RNA viral analysis, antigens, viral analysis, defective
viruses genetics, Diptera microbiology, ducks microbiology, avian
genetics, avian immunology, swine microbiology, viral interference, virus
replication.
Bean, W.J., S.C. Threlkeld, and R.G. Webster (1989). Biologic
potential of amantadine-resistant influenza A virus in an avian model. Journal
of Infectious Diseases 159(6): 1050-6.
ISSN: 0022-1899.
NAL
Call Number: 448.8 J821
Abstract: Amantadine has been accepted for both the
treatment and prophylaxis of influenza A virus infections. Although
amantadine-resistant mutants have been shown to be readily generated both in
the laboratory and in children treated with rimantadine, little is known about
their biologic properties, such as genetic stability, transmissibility, or
pathogenicity, compared with the parental virus. This study examined these
properties using an avian influenza virus, A/chicken/Pennsylvania/1370/83
(H5N2). Variants that were amantadine-resistant, virulent, and capable of
competing with wild-type virus for transmission to susceptible hosts in the
absence of the drug were selected. These amantadine-resistant variants were
also genetically stable, showing no reversion to wild-type after six passages
in birds over a period of greater than 20 d. Thus, these virus variants had no
detectable biologic impairment. The mutations conferring drug resistance were
in the M2 polypeptide and were identical to mutations previously described in
human amantadine-resistant virus. These results suggest that resistant mutants
may have the potential to threaten the effective use of amantadine and
rimantadine for the control of epidemic influenza.
Descriptors: amantadine pharmacology, fowl plague
microbiology, influenza A virus avian drug effects, amantadine therapeutic use,
chickens, drug resistance, microbial, fowl plague drug therapy, fowl plague
transmission, avian genetics, avian pathogenicity, mutation, RNA viral
genetics, virulence.
Beard, C.W., M. Brugh, and R.G. Webster (1987). Emergence
of amantadine-resistant H5N2 avian influenza virus during a simulated layer
flock treatment program. Avian Diseases 31(3): 533-7. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: An experiment was designed to simulate field
conditions in which preventive treatment is not initiated until after some
chickens in a flock are infected with avian influenza (AI). Twelve hens began
to receive amantadine hydrochloride on the day they were inoculated (day 0)
with highly pathogenic AI virus, A/chicken/Pa/1370/83. These hens remained
clinically normal through 8 days postinoculation (PI), but five died after day
9; mean death time (MDT) was 18 days. Three of 12 hens given amantadine
beginning 1 day PI died (MDT 5.4 days), seven of 12 hens given amantadine
beginning 3 days PI died (MDT 3.7 days), and all 12 inoculated hens not given
amantadine died (MDT 4.9 days). The delayed mortality in the day 0 treatment
group was likely due not to the original inoculum but to the emergence of a
drug-resistant virus population. Virus isolated from a dead hen from that group
was resistant to the actions of amantadine in both in ovo and in vivo tests.
The lack of late mortality due to the drug-resistant virus in the day 1 and day
3 treatment groups, which were in close contact with the day 0 treatment group,
was attributed to their becoming infected before treatment with the drug and to
the development of protective immunity.
Descriptors: amantadine pharmacology, chickens, fowl
plague prevention and control, influenza A virus avian drug effects, amantadine
therapeutic use, chick embryo, drug resistance, microbial, fowl plague drug
therapy.
Becht, H. (1971). Cytoplasmic synthesis of an
arginine-rich nuclear component during infection with an influenza virus. Journal
of Virology 7(2): 204-7. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Descriptors: arginine metabolism, cultured cells
metabolism, cytoplasm metabolism, influenza A virus avian pathogenicity,
proteins biosynthesis, autoradiography, cell line, cell nucleus metabolism,
chick embryo, ethanol, fibroblasts, hamsters, hydrochloric acid, kidney,
precipitation, solvents, trichloroacetic acid, tritium.
Becht, H. (1969). Induction of an arginine-rich
component during infection with influenza virus. Journal of General
Virology 4(2): 215-20. ISSN:
0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: arginine metabolism, influenza A virus avian
metabolism, tissue culture, autoradiography, cell nucleus metabolism, chick
embryo, cytoplasm metabolism, dactinomycin pharmacology, fibroblasts, leucine
metabolism, lysine metabolism, tritium, virus replication.
Becht, H. (1968). Properties of erythrocytes
stabilized with sulfosalicylic acid and their use in an indirect hemagglution test
with influenza virus RNP-antigen. Journal of Immunology 101(1):
18-22. ISSN: 0022-1767.
NAL
Call Number: 448.8 J8232
Descriptors: antigens, erythrocytes, hemagglutination
tests, indicators and reagents, orthomyxoviridae, salicylic acids, sulfonic acids,
complement fixation tests, immune sera, influenza A virus avian,
nucleoproteins, sheep.
Becht, H. (1971). Untersuchungen uber die
Biosynthese und uber den serologischen Nachweis des Ribonucleoproteid-Antigens
von Influenzaviren. I. Untersuchungen uber die Bildung des RNP-Antigens und die
Rolle des Zellerns bei seiner Synthese. [Studies on biosynthesis and
serological demonstration of ribonucleoprotein antigen of influenza viruses. I.
Studies on biosynthesis of RNP antigen and the role of cell nucleus in its
synthesis]. Zeitschrift Fur
Medizinische Mikrobiologie Und Immunologie 156(4): 309-30. ISSN: 0044-3077.
NAL
Call Number: 449.8 Z3
Descriptors: antigens biosynthesis, influenza A virus
avian immunology, antigens, viral biosynthesis, arginine, autoradiography, AZO
compounds pharmacology, cell nucleus metabolism, chick embryo, fibroblasts,
hemagglutinins viral biosynthesis, membranes, nucleoproteins biosynthesis,
ribose, serotyping, viral proteins biosynthesis.
Becht, H. and R. Drzeniek (1968). The effect of
azo dyes on myxovirus neuraminidase and on virus multiplication. Journal
of General Virology 2(2): 261-8.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: azo compounds pharmacology, influenza A virus
avian drug effects, neuraminidase antagonists and inhibitors, Newcastle disease
virus drug effects, arboviruses drug effects, arboviruses growth and
development, chick embryo, complement fixation tests, Congo red pharmacology,
hemagglutination tests, avian growth and development, neuraminidase metabolism,
Newcastle disease virus growth and development.
Becht, H., H. Gruschkau, and R. Rott (1979). The M
protein of influenza viruses has no immunizing effect. Medical
Microbiology and Immunology 167(4): 285-8.
ISSN: 0300-8584.
Abstract: Influenza A virus M protein was prepared by
electrophoresis in SDS polyacrylamide gel from virus particles which had been
pretreated with octylglucoside to remove the surface glycoproteins; M antigens
from the influenza virus strains A/Victoria/3/75 (H3N2), A/FPV/Rostock (Hav1N1)
and A/chick/Germany/49 (Hav2Neq1) did not protect mice against a lethal
challenge infection with the virulent Victoria strain.
Descriptors: antigens, viral immunology, influenza A virus
avian immunology, human immunology, viral proteins immunology, antibodies,
viral biosynthesis, hemagglutination inhibition tests, immunization, influenza
immunology, influenza prevention and control, mice.
Becht, H. and B. Malole (1975). Comparative
evaluation of different fixation procedures and different coupling reagents for
the demonstration of influenza virus-specific antibodies by the indirect
hemagglutination test. Medical Microbiology and Immunology 162(1):
43-53. ISSN: 0300-8584.
Abstract: The indirect hemagglutination technique has
been improved by fixing the carrier erythrocytes successively with
glutaraldehyde and sulfosalicylic acid. Sensitization by covalent conjugation
of influenza virus antigens to the erythrocytes with various coupling reagents,
which resulted in stable and highly sensitive test cells, has been defined. An
economical affinity chromatography procedure using antibody-coated agarose has
been developed to prepare sufficiently pure antigens from fowl plague virus-infected
choriollantoic membranes.
Descriptors: antibodies, viral analysis, erythrocytes
immunology, hemagglutination tests methods, antibody specificity, blood
preservation, chromatography, affinity, cytological techniques, glutaral,
hemagglutinins viral isolation and purification, influenza A virus avian
immunology, salicylic acids.
Becht, H., R. Rott, and H.D. Klenk (1972). Effect
of Concanavalin A on cells infected with enveloped RNA viruses. Journal
of General Virology 14(1): 1-8.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: agglutination drug effects, lectins
pharmacology, RNA viruses, agglutination tests, arboviruses, cattle, cell line,
cell membrane drug effects, cultured cells microbiology, chick embryo,
concanavalin A pharmacology,
fibroblasts, hamsters, HeLa cells microbiology, influenza A virus avian,
kidney, cell line microbiology, Newcastle disease virus, orthomyxoviridae,
polioviruses, Semliki Forest virus, simian virus 40, sindbis virus, vesicular
stomatitis Indiana virus, virus diseases.
Bektemirov, T.A., S.A. Moisiadi, E.N. Kantorovich,
N.V. Kaverin, and O.N. Berezina (1974). Nekotorye biologicheskie svoistva
"nepol'nogo" virusa grippa. [Biological properties of
"incomplete" influenza virus]. Voprosy Virusologii (2):
181-4. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: defective viruses pathogenicity, orthomyxoviridae
pathogenicity, influenza A virus avian, interferons biosynthesis, mice, viral
interference, virus replication.
Belshe, R.B. (1995). A review of attenuation of
influenza viruses by genetic manipulation. American Journal of
Respiratory and Critical Care Medicine 152(4, Pt. 2): S72-5. ISSN: 1073-449X.
Descriptors: genetic engineering methods, influenza A
virus human genetics, influenza B virus genetics, influenza vaccine genetics,
adult, infant, avian immunology, human immunology, human pathogenicity,
influenza B virus immunology, influenza B virus pathogenicity, influenza
vaccine immunology, vaccines, attenuated genetics, vaccines, attenuated
immunology, vaccines, combined genetics,
vaccines, combined immunology.
Bergelson, L.D., A.G. Bukrinskaya, N.V. Prokazova,
G.I. Shaposhnikova, S.L. Kocharov, V.P. Shevchenko, G.V. Kornilaeva, and E.V.
Fomina Ageeva (1982). Role of gangliosides in reception of influenza virus.
European Journal of Biochemistry FEBS 128(2-3): 467-74. ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: The ganglioside composition of Ehrlich
ascites carcinoma (EAC) cells and the role of the individual gangliosides in
binding and penetration into the cell of influenza virus were determined. EAC
gangliosides identical with or close to GM3, GM2, GM1, GT1a and GT1b were
characterized by thin-layer chromarography, compositional analyses, methylation
analysis and mass-spectrometry. The ganglioside uptake capacity of native and
neuraminidase-treated EAC cells was studied with tritium-labeled gangliosides
of definite structure and the binding of influenza virus to cells was
determinated by using [3H]uridine-labeled virus and by hemagglutination
studies. Treatment of the cells with Vibrio cholerae neuraminidase largely
decreased binding of the virus. Exogenous gangliosides with a terminal
galactose unit or a penultimate galactose masked by neuraminic acid were able
to restore the virus-binding capacity of neuraminidase-treated cells, however,
the main ganglioside of EAC cells, GM2, which carbohydrate chain is terminated
by N-acetylgalactosamine, was completely ineffective. The common carbohydrate
sequence of the gangliosides showing binding activity (formula; see text) is
proposed to be the main recognition structure of the influenza virus receptor
on the surface of EAC cells. Penetration of labeled influenza virus into the
nuclei of EAC cells was evaluated by measuring the radioactivity of the nuclei
of neuraminidase-treated ganglioside-loaded cells after exposition to the
labeled virus. Of all gangliosides tested only trisialogangliosides of the GT1b
type were able to induce increased entry of the virus into the cells and
accumulation of its radioactive component into the nuclei. It is suggested that
GT1b gangliosides react specifically with the virus protein responsible for
membrane fusion (apparently the hemagglutinin HA2 subunit) and thus are
involved in virus penetration and delivery of the virus genome to the nuclei.
Descriptors: carcinoma, ehrlich tumor microbiology,
gangliosides metabolism, influenza A virus avian physiology, receptors, virus
metabolism, carbohydrate sequence, hemagglutination tests, kinetics, mice,
neuraminidase pharmacology, receptors, virus drug effects, structure activity
relationship, vibrio cholerae enzymology.
Berting, A., C. Fischer, S. Schaefer, W. Garten, H.D.
Klenk, and W.H. Gerlich (2000). Hemifusion activity of a chimeric influenza
virus hemagglutinin with a putative fusion peptide from hepatitis B virus. Virus
Research 68(1): 35-49. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: Entry of enveloped viruses is often mediated
by an aminoterminal hydrophobic fusion peptide of a viral surface protein. The
S domain of the hepatitis B virus surface protein contains a putative fusion
peptide at position 7-18, but no systems are available to study its function
directly. We tested the functionality of this peptide and a related peptide
from another hepadnavirus in the context of the well-characterized influenza
virus hemagglutinin H7 using gene mutation. The chimeric hemagglutinins could
be expressed stably in CV 1 cells and were transported to the cell surface. The
chimeras were incompletely cleaved by cellular proteases but cleavage could be
completed by trypsin treatment of the cells. The chimeras did not differ in
receptor binding, i.e. erythrocyte binding. Hemifusion and fusion pore
formation were detected with membrane or cytosolic fluorescent dye-labeled
erythrocytes as target structures of the hemagglutinin. Five of six different
chimeras mediated hemifusion in 20-54% of the hemagglutinin-expressing cells,
complete fusion and syncytium formation was not observed. The data suggest that
the sequence 7-18 of the hepatitis B S domain may indeed initiate the first
step of viral entry, i.e. hemifusion.
Descriptors: hemagglutinin glycoproteins, influenza virus
metabolism, hepatitis B virus metabolism, membrane fusion, viral fusion
proteins metabolism, amino acid sequence, cell line, chimeric proteins
genetics, chimeric proteins metabolism, hemagglutinin glycoproteins, influenza
virus genetics, hepatitis B virus genetics, molecular sequence data, peptides
chemistry, peptides genetics, receptors, virus metabolism, viral fusion
proteins chemistry, viral fusion proteins genetics.
Betakova, T., F. Ciampor, and A.J. Hay (2005). Influence
of residue 44 on the activity of the M2 proton channel of influenza A virus.
Journal of General Virology 86(Pt. 1): 181-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The influenza A virus M2 proton channel plays
a role in two stages of virus replication. The proteins of two closely related
strains of the avian H7 subtype of influenza A virus, Rostock and Weybridge,
were found to differ in their pH-modulating activities and activation
characteristics. Of three amino acid differences at residues 27, 38 and 44
within the membrane-spanning domain, substitution at residue 44 was necessary
and sufficient to account for differences in trans-Golgi pH-modulating
activity, whereas changes in all three were required to switch the activation
characteristics of the Weybridge M2 to those of the Rostock M2. These results
not only separate the two phenomena genetically, but also indicate that the
'unique' activation characteristics of the Rostock M2 channel were selected
specifically. In addition, they point to the importance of functional
complementarity between the activation characteristics of the M2 channel and
the pH of membrane fusion by haemagglutinin during virus entry.
Descriptors: influenza A virus, avian metabolism, ion
channels metabolism, viral matrix proteins metabolism, amino acid sequence,
cell line, Golgi apparatus chemistry, Golgi apparatus metabolism,
hemagglutinins, viral metabolism, hydrogen-ion concentration, ion channels
chemistry, molecular sequence data, protein structure, tertiary, protons,
sequence alignment, viral matrix proteins chemistry, virus replication.
Blagoveshchenskaya, O.V. and Y.Z. Ghendon (1978). Comparative
study of virion transcriptase of some influenza virus strains. Acta
Virologica 22(2): 97-103. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The activities, the temperature and pH optima
of in vitro functioning and stability upon heating of virion transcriptase of
10 human influenza virus A strains differing in reactogenicity and isolated in
different epidemiological situations, and of fowl plague virus (FVP) were
compared. As compared with virion transcriptase of human influenza virus
strains studied, that of FPV had a higher pH optimum, was capable of
functioning in vitro at a higher temperature and was more stable on heating.
Freshly isolated and vaccine influenza virus strains on the one hand and
strains isolated at the peak and in the end of an epidemic did not differ in
the virion transcriptase properties. The virion transcriptase of a strain
isolated from a local influenza outbreak was much less active than
transcriptase of a highly epiedmic strain.
Descriptors: influenza A virus avian enzymology, human
enzymology, RNA nucleotidyltransferases metabolism, RNA replicase metabolism,
heat, hydrogen-ion concentration, influenza vaccine, species specificity,
temperature, virion enzymology.
Blinov, V.M., O.I. Kiselev, S.M. Resenchuk, A.I.
Brovkin, A.G. Bukrinskaia, and L.S. Sandakhchiev (1993). Analiz
potentsial'nykh uchastkov rekombinatsii v genakh gemaggliutinina virusov grippa
zhivotnykh v otnoshenii ikh adaptatsii k novomu khoziainu--cheloveku. [An
analysis of the potential areas of recombination in the hemagglutinin genes of
animal influenza viruses in relation to their adaptation to a new host--man].
Voprosy Virusologii 38(6): 263-8.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The authors tried to decode the mechanism of
influenza viruses species adaptation in the process of host changing. The
functionally important replacement in the surface pocket domains were revealed,
particularly in the conservative region 221-241, involving fibronectin-like
part. Close replacements were revealed in the region 141-161. The method of
construction of heteroduplexes between hemagglutinin RNA of duck, pig, and
human viruses was used. The method showed that all heteroduplexes formed
recombinogene structures. An unexpected effect of directional recombination was
elicited for hemagglutinin RNA heteroduplexes in cases of duck-pig and
human-pig viruses. During the directional recombination the following processes
took place: the receptor-binding site of animal type was transmitted to the
duck virus, while the human receptor-binding site was transmitted to the pig
virus. According to the experimental data, a new hypothesis is formulated: the
cascade mechanism of directional recombination for duck, animal and human
viruses makes it possible for the recombinant viruses to overcome interspecies
barriers.
Descriptors: adaptation, physiological genetics, genes
viral genetics, hemagglutinins viral genetics, influenza A virus avian
genetics, porcine genetics, recombination, genetic genetics, amino acid
sequence, ducks microbiology, human genetics, molecular sequence data, nucleic acid heteroduplexes genetics, RNA
viral genetics, swine microbiology, variation genetics genetics.
Blinova, V.K., R.Y. Podchernyaeva, and M.I. Sokolov
(1975). K voprosu rekombinatsii virusov grippa cheloveka i dikikh ptits.
[Recombination of influenza viruses from man and wild birds (terns)]. Sbornik
Trudov Institut Virusologii Imeni D.I. Ivanovskogo, "Ekologiya
Virusov" (3): 31-35.
Descriptors: influenza viruses, wild birds, terns, humans,
virus recombination.
Bogautdinov, Z.F. (1977). Fermentingibiruyushchaya
aktivnost spetsificheskoi syvorotki k neiraminidaze virusa grippa ptitsy.
[Enzyme inhibiting activity of specific serum against the neuraminidase of
avian influenza virus]. Doklady Vsesoyuznoi Akademii
Sel'Skokhozyaistvennykh Nauk (4): 29-30.
Descriptors: avian influenza virus, DEAE cellulose,
neuraminidase, chromatography.
Bogautdinov, Z.F. (1977). Immunoenzymology of the
neuraminidase of avian influenza virus complexed with a substrate and
antibodies. Soviet Agricultural Sciences (10): 39-41. ISSN: 0735-2700.
NAL
Call Number: S1.S68
Descriptors: avian influenza virus, neuraminidase,
immunoenzymology, antibodies.
Bogautdinov, Z.F. and I.G. Lavrova (1976). Izuchenie
svyazi mezhdu antigennoi spetsifichnost'yu i fiziko-khimicheskimi svoistvami
neiraminidaz. [Relationship between antigenic specificity and physico-chemical
properties of neuraminidases of avian influenza viruses]. Doklady
Vsesoyuznoi Akademii Sel'Skokhozyaistvennykh Nauk (1): 37-38.
Descriptors: avian influenza viruses, neuraminidase,
antigens, physio-chemical properties, techniques.
Bonin, J. and C. Scholtissek (1983). Mouse
neurotropic recombinants of influenza A viruses. Archives of Virology
75(4): 255-68. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Recombinants with known gene constellations
between fowl plague virus (FPV) and various prototype influenza virus strains
have been examined for neurovirulence in suckling mice. Strongly neurotropic
recombinants were obtained from crosses between FPV and the strains virus N,
Hong Kong, and PR8, but not between FPV and equi 2 or swine viruses. All highly
neurotropic recombinants had RNA segment 4 (HA) derived from FPV and RNA
segment 2 (Ptra gene) from the other prototype strain. The derivation of two other
RNA segments of the polymerase complex, namely RNA segments 3 (Pol 2) and 5
(NP) and also segment 8 (NS) can modulate these properties. For example, if in
recombinants between FPV and virus N in addition to RNA segment 2 also RNA
segments 3 and/or 8 are derived from virus N, neurovirulence is further
enhanced, while replacement of RNA segment 5 of FPV by the corresponding
segment of virus N decreases or abolishes neurovirulence. The derivation of the
other genes does not seem to be relevant for neurovirulence in the crosses
mentioned above. Of the prototype strains tested, the turkey England (t. Engl.)
strain is the only one which was highly neurotropic for suckling mice.
Recombinants between FPV and t. Engl. which have kept the HA gene of t. Engl. were
still neurotropic, while those with the HA gene of FPV were completely
avirulent. The results obtained demonstrated that 1. the creation of influenza
virus recombinants neurotropic for mice is not a rare event; 2. one of the
parents should multiply well in mouse lungs; 3. the presence of a cleavable
hemagglutinin is necessary, but not sufficient. In the pair FPV/turkey England
the hemagglutinin of turkey England seems to determine neurovirulence.
Descriptors: influenza A virus, genetics, recombination, genetic,
brain microbiology, cultured cells, embryo microbiology, fibroblasts, genes
viral, avian genetics, pathogenicity, kidney, lung microbiology, mice,
virulence.
Borek, A. and C. Sauter (1975). Fowl plague virus
adapted to human leukemia cells: interaction with normal human leukocytes and
plastic surfaces. Pathologia Et Microbiologia 43(1): 62-73. ISSN: 0031-2959.
NAL
Call Number: 448.8 Sch9
Abstract: An avian influenza A virus which grows well
in human leukemic myeloblasts was unable to replicate in normal human
leukocytes. The virus adhered during the first hours of incubation to plastic
surfaces and to leukocytes and was then released into the supernatant; care
should be taken not to confuse this with viral growth.
Descriptors: influenza A virus, avian growth and
development, leukocytes microbiology, adaptation, physiological, adsorption,
adult, cell adhesion, granulocytes microbiology, leukemia, myelocytic, acute,
lymphocytes microbiology, monocytes microbiology, plastics, tissue culture, virus
replication.
Borland, R. and B.W. Mahy (1968). Deoxyribonucleic
acid-dependent ribonucleic acid polymerase activity in cells infected with
influenza virus. Journal of Virology 2(1): 33-9. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Descriptors: DNA, viral metabolism, fibroblasts
enzymology, influenza A virus avian metabolism, RNA biosynthesis, RNA
nucleotidyltransferases biosynthesis, chick embryo, dactinomycin pharmacology,
hemagglutination, viral, RNA viral biosynthesis, tissue culture, virus replication.
Borland, R. and B.W. Mahy (1970). RNA and protein
synthesis in chick embryo lung cell monolayer cultures infected with influenza
virus. Archiv Fur Die Gesamte Virusforschung 30(4): 367-78. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: cytopathogenic effect, viral, lung
metabolism, orthomyxoviridae pathogenicity, proteins biosynthesis, RNA
biosynthesis, tissue culture, carbon isotopes, centrifugation, density
gradient, chick embryo, dactinomycin pharmacology, hemadsorption, hemagglutination,
influenza A virus avian growth and development, avian pathogenicity, lung
pathology, orthomyxoviridae growth and development, species specificity,
sucrose, tritium, uridine metabolism, valine metabolism, virus replication.
Bosch, F.X. (1985). Studies on the development of
the charge heterogeneity of the influenza virus glycoproteins. Archives
of Virology 83(3-4): 311-7. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The heterogeneity in charge of the influenza
virus glycoproteins, hemagglutinin (HA) and neuraminidase (NA) is retained,
when glycosylation is inhibited by tunicamycin (TM) or 2-deoxyglucose (2-dg).
This is in contrast to the charge heterogeneity of the G protein of vesicular
stomatitis virus (VSV), which is mainly due to heterogeneous sulfation of the
carbohydrate side chains and therefore is abolished by the above mentioned
inhibitors of glycosylation. Thus, the charge heterogeneity of influenza virus
glycoproteins might be attributable to some as yet unidentified modifications
of the polypeptide backbone.
Descriptors: hemagglutinins viral, influenza A virus avian
analysis, membrane glycoproteins, neuraminidase, viral envelope proteins, viral
proteins, cultured cells, chick embryo, deoxyglucose pharmacology,
electrophoresis, polyacrylamide gel, hemagglutinin glycoproteins, influenza
virus, avian enzymology, avian metabolism, human analysis, isoelectric
focusing, isoelectric point, translation, genetic, tunicamycin pharmacology,
vesicular stomatitis Indiana virus analysis.
Bosch, F.X., W. Garten, H.D. Klenk, and R. Rott
(1981). Proteolytic cleavage of influenza virus hemagglutinins: primary
structure of the connecting peptide between HA1 and HA2 determines proteolytic
cleavability and pathogenicity of Avian influenza viruses. Virology
113(2): 725-35. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: hemagglutinins viral analysis, influenza A
virus avian immunology, peptide hydrolases metabolism, amino acid sequence,
human immunology, human pathogenicity, isoelectric point.
Bosch, F.X., A. Mayer, and R.T. Huang (1980). Simple
and rapid separation of ortho- and paramyxovirus glycoproteins. Medical
Microbiology and Immunology 168(4): 249-59.
ISSN: 0300-8584.
Abstract: The hemagglutinin (HA) and neuraminidase (NA)
of influenza viruses, as well as the fusion protein (F) and
hemagglutinin-neuraminidase (HN) of paramyxoviruses, have been separated in
native form using a two-step procedure. The glycoproteins are efficiently
extracted from virions using the on-ionic detergent octyl-beta-D-glucoside and
are then applied to a column of agarose beads coupled with tyrosine-sulfanilic
acid. Pure HA and F are obtained in good yield in the flow-through from this
column. NA and HN bind strongly and can be eluted, albeit somewhat contaminated
with HA or F, by raising the pH of the column buffer. The separated
non-denatured fractions can be used for structural, functional, and antigenic
studies.
Descriptors: glycoproteins isolation and purification,
influenza A virus avian analysis, human analysis, Newcastle disease virus
analysis, viral proteins isolation and purification, chromatography, affinity,
detergents, hemagglutinins viral isolation and purification, neuraminidase
isolation and purification.
Bosch, F.X., M. Orlich, G. Legler, R.T. Schwarz, and
R. Rott (1984). Effect of inhibitors of glycosylation on proteolytic
activation of avian influenza virus hemagglutinins: discrimination between
tryptic cleavage and elimination of the connecting peptide. Virology
132(1): 199-204. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The glycosylation inhibitors tunicamycin
(TM), 2-deoxyglucose (2-dg), bromoconduritol (BC; 3,5/4,6-6-bromo
3,4,5-trihydroxycyclohex-1-ene), and N-methyl-deoxynojirimycin (MdN) have been
used to study the role of glycosylation in the two proteolytic reactions
involved in the biological activation of H7 influenza virus hemagglutinins
(HAs): trypsinlike cleavage and subsequent elimination of the connecting
peptide. The results obtained revealed that trypsin-like cleavage of the HAs of
pathogenic strains does not require glycosylation, since these HAs were
efficiently cleaved in the presence of TM and 2-dg. The elimination of the
connecting peptide between HA1 and HA2, however, appears to require the transfer
of oligosaccharides onto the HA polypeptide, since this activity was blocked by
TM and by 2-dg. Elimination was not blocked by BC or MdN, which inhibit glucose
trimming and subsequent conversion of the high-mannose type to the complex type
of carbohydrate.
Descriptors: 1 deoxynojirimycin analogs and derivatives,
carbohydrates metabolism, hemagglutinins viral metabolism, influenza A virus
avian analysis, trypsin metabolism, deoxyglucose pharmacology, glucosamine
analogs and derivatives, glucosamine pharmacology, inositol analogs and
derivatives, inositol pharmacology, tunicamycin pharmacology, virion analysis.
Bosch, F.X., V. Von Hoyningen Huene, C. Scholtissek,
and R. Rott (1982). The overall evolution of the H7 influenza virus
haemagglutinins is different from the evolution of the proteolytic cleavage
site. Journal of General Virology 61(Pt. L): 101-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: It has been shown previously that the
pathogenicity of avian influenza A viruses depends strictly on the proteolytic
cleavability of their haemagglutinins (HAs) in infected cells. In this
communication, pathogenic and non-pathogenic strains of the H7 subtype have
been studied by comparing the genetic relatedness of their HA genes. Some of
the cleavable HAs of pathogenic strains were genetically more closely related
to the uncleaved HAs than to other cleavable HAs. These data clearly
demonstrate that the overall evolution of the H7 haemagglutinins is different
from the evolution of the specific cleavage site.
Descriptors: genes viral, hemagglutinins viral genetics,
influenza A virus avian immunology, evolution, hemagglutinins viral analysis,
avian genetics, avian pathogenicity, nucleic acid hybridization.
Bossart Whitaker, P., M. Carson, Y.S. Babu, C.D.
Smith, W.G. Laver, and G.M. Air (1993). Three-dimensional structure of
influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy
2,3-dehydro-N-acetyl neuraminic acid. Journal of Molecular Biology
232(4): 1069-83. ISSN: 0022-2836.
NAL
Call Number: 442.8 J8224
Abstract: We present here the three-dimensional
structure of neuraminidase (E.C. 3.2.1.18) from influenza virus
A/Tern/Australia/G70c/75 (N9), determined by the method of multiple isomorphous
replacement, and the structure of the neuraminidase complexed with an
inhibitor, 2-deoxy-2,3-dehydro-N-acetyl neuraminic acid (DANA). Native and
inhibitor complex crystals are isomorphous and belong to space group I432 with
unit cell dimensions of 183.78 A. The native enzyme structure and the inhibitor
complex structure have been refined at 2.5 A and 2.8 A resolution,
respectively, with crystallographic R-factor values of 0.193 for the native
enzyme, and 0.179 for the inhibitor complex. The current enzyme model includes
387 amino acid residues which comprise the asymmetric unit. The
root-mean-square deviation from ideal values is 0.013 A for bond lengths and
1.6 degree for bond angles. The neuraminidase (NA), as proteolytically cleaved
from the virus, retains full enzymatic and antigenic activity, and is a
box-shaped tetramer with edge lengths of 90 A and a maximal depth of 60 A. The
NA tetramers are composed of crystallographically equivalent monomers related
by circular 4-fold symmetry. Each monomer folds into six antiparallel
beta-sheets of four strands. The secondary structure composition is 50%
beta-sheet. The remaining 50% of the residues form 24 strand-connecting loops
or turns. One of the loops contains a small alpha-helix. The structure of the
complex of NA with DANA, a transition state analog, has enabled us to identify
and characterize the site of enzyme catalysis. The center of mass of bound
inhibitor is 32 A from the 4-fold axis of the tetramer, lodged at the end of a
shallow crater of diameter 16 A with a depth of 8 to 10 A. There are 12 amino
acid residues that directly bind DANA, with a further six conserved amino acids
lining the active site pocket. The neuraminidase inhibitor complex provides a
three-dimensional model which will be used to further the understanding of
enzymatic hydrolysis and aid the design of specific, antineuraminidase
antiviral compounds.
Descriptors: influenza A virus avian enzymology,
neuraminidase antagonists and inhibitors, neuraminidase chemistry, sialic acids
chemistry, binding sites, influenza B virus enzymology, mercury chemistry,
models, molecular, molecular conformation, N-acetylneuraminic acid, platinum
chemistry, protein conformation, sialic acids metabolism, x-ray diffraction.
Brecht, H., U. Hammerling, and R. Rott (1971). Undisturbed
release of influenza virus in the presence of univalent antineuraminidase
antibodies. Virology 46(2): 337-43.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: antibodies, influenza A virus avian growth
and development, neuraminidase isolation and purification, neuraminidase
metabolism, orthomyxoviridae growth and development, centrifugation, density
gradient, chick embryo, chromatography, DEAE-cellulose, fibroblasts,
hemagglutination tests, immune sera, immunoglobulin g, immunoglobulins, avian
enzymology, avian immunology, avian pathogenicity, neuraminic acids
biosynthesis, orthomyxoviridae enzymology, orthomyxoviridae immunology,
orthomyxoviridae pathogenicity, rabbits, sucrose, tissue culture, virus
replication.
Breslin, J.J., L.G. Smith, and J.S. Guy (2001). Baculovirus
expression of turkey coronavirus nucleocapsid protein. Avian Diseases
45(1): 136-43. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The nucleocapsid (N) gene of turkey
coronavirus (TCV) was amplified by reverse transcriptase-polymerase chain
reaction, cloned, and expressed in the baculovirus expression system. A
recombinant baculovirus containing the TCV N gene (rBTCV/N) was identified by
polymerase chain reaction and expression of TCV N protein as determined by
western immunoblot analysis. Two TCV-specific proteins, 52 and 43 kDa, were
expressed by rBTCV/N; one of these proteins, p52, was comparable in size to
native TCV N protein. Baculovirus-expressed N proteins were used as antigen in
an indirect enzyme-linked immunosorbent assay (ELISA) for detection of
TCV-specific antibodies. The ELISA detected antibodies specific for TCV and
infectious bronchitis virus, a closely related avian coronavirus, but did not
detect antibodies specific for other avian viruses (avian influenza, avian
reovirus, avian paramyxovirus 3, avian adenovirus 1, or Newcastle disease
virus). These findings indicate that baculovirus-expressed TCV N protein is a
suitable source of antigen for ELISA-based detection of TCV-specific antibodies
in turkeys.
Descriptors: baculoviridae metabolism, nucleocapsid
biosynthesis, nucleocapsid proteins, turkeys virology, enteritis veterinary,
enteritis virology, enzyme linked immunosorbent assay veterinary, North
Carolina, nucleocapsid genetics, poultry diseases virology, reverse
transcriptase polymerase chain reaction veterinary.
Breuning, A. and C. Scholtissek (1986). A
reassortant between influenza A viruses (H7N2) synthesizing an enzymatically
inactive neuraminidase at 40 degrees which is not incorporated into infectious
particles. Virology 150(1): 65-74.
ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Cells infected with a reassortant (113/Ho,
H7N2) between A/fowl plague/Rostock/34 (FPV, H7N1) and A/Hong Kong/1/68 (H3N2)
carrying RNA segments 1 and 6 of the Hong Kong virus and the residual genes of
FPV, synthesized at 40 degrees a neuraminidase (NA) which is enzymatically not
active and which is not incorporated into infectious particles. At 40 degrees
NA accumulates in the rough endoplasmic reticulum. It contains mainly
carbohydrate side chains of the mannose type, and fucose is only scarcely
incorporated. At 33 degrees NA of the reassortant is overproduced, and at least
some of it is active and is incorporated into viral particles. Under
nonreducing conditions during PAGE its NA migrates to the same position as
after heating with mercaptoethanol, in contrast to the Hong Kong parent virus.
It is speculated that at 40 degrees the tetramerization of the NA in the rough
endoplasmic reticulum does not function, and in this way its migration to the
cytoplasmic membrane and its incorporation into infectious particles does not
occur. Since 113/Ho is as pathogenic for the chicken (body temperature of 41
degrees) as is FPV, the question arises which role the NA plays in virus
replication and spread in the infected organism.
Descriptors: influenza A virus avian genetics, human
genetics, neuraminidase genetics, carbohydrate sequence, cell compartmentation,
chick embryo, glycopeptides analysis, glycoproteins genetics, glycoproteins
metabolism, hemagglutinins viral genetics, avian enzymology, influenza A virus
human enzymology, mutation, neuraminidase metabolism, recombination, genetic,
temperature, viral proteins metabolism, virus replication.
Briedis, D.J., G. Conti, E.A. Munn, and B.W. Mahy
(1981). Migration of influenza virus-specific polypeptides from cytoplasm to
nucleus of infected cells. Virology 111(1): 154-64. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: cell nucleus metabolism, cytoplasm
metabolism, influenza A virus avian metabolism, viral proteins metabolism,
capsid metabolism, cell fractionation, cell line, dogs, avian growth and
development, kinetics.
Bromley, P.A. and R.D. Barry (1973). Characterization
of the ribonucleic acid of fowl plague virus. Archiv Fur Die Gesamte
Virusforschung 42(2): 182-96. ISSN:
0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian analysis, RNA viral
analysis, autoradiography, base sequence,
centrifugation, density gradient, chick embryo, chromatography,
DEAE-cellulose, chromatography, gel, densitometry, electrophoresis,
polyacrylamide gel, influenza A virus avian isolation and purification, nucleic
acid denaturation, phosphorus isotopes, RNA viral isolation and purification,
ribonucleases, tissue culture, virus cultivation.
Bromley, P.A. and R.D. Barry (1970). Studies on
the nature of influenza virus ribonucleic acid. Journal of General
Microbiology 63(3): xvi. ISSN:
0022-1287.
NAL
Call Number: 448.3 J823
Descriptors: influenza A virus avian analysis, RNA viral
analysis, base sequence, guanine analysis.
Bron, R., A.P. Kendal, H.D. Klenk, and J. Wilschut
(1993). Role of the M2 protein in influenza virus membrane fusion: effects
of amantadine and monensin on fusion kinetics. Virology 195(2):
808-11. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: We have investigated the effects of the
anti-influenza drug amantadine (AMT) and the proton-ionophore monensin on the
membrane fusion activity of influenza virus in a liposomal model system, using
a kinetic fluorescence lipid mixing assay. Fusion of influenza virus
A/turkey/Oregon/71 (H7N3) with liposomes was slowed down in the presence of 2
microM AMT. The effect of AMT was not observed with an AMT-resistant mutant
virus. Fusion inhibition by AMT was reversed by the proton-ionophore monensin.
In fact, 1 microM monensin stimulated fusion of AMT-sensitive or -resistant
virus, irrespective of the presence of AMT. The effects of AMT and monensin
increased with increasing temperature. They were not observed at 25 degrees,
but were very prominent at 45 degrees. Monensin did not influence the fusion
rates of reconstituted viral envelopes (virosomes), which lack the nucleocapsid
and the M1 protein. These results suggest that intraviral low pH facilitates
influenza virus fusion, possibly by weakening interactions of the C-terminus of
the viral hemagglutinin with the M1 protein and/or the viral nucleocapsid. The
effect of AMT on the fusion capacity of influenza virus may contribute to the
anti-influenza action of the drug in the early stages of cellular infection.
However, the limited extent of the fusion inhibition suggests that the fusion
step is unlikely to be the primary target of AMT.
Descriptors: amantadine pharmacology, influenza A virus
avian metabolism, monensin pharmacology, viral matrix proteins metabolism,
electrophoresis, polyacrylamide gel, immunoblotting, avian drug effects,
kinetics, membrane fusion drug effects.
Brooks, M.J., J.J. Sasadeusz, and G.A. Tannock (
2004). Antiviral chemotherapeutic agents against respiratory viruses: where
are we now and what's in the pipeline? Current Opinion in Pulmonary
Medicine 10(3): 197-203. ISSN:
1070-5287.
Abstract: PURPOSE OF REVIEW: The emergence of severe
acute respiratory syndrome in late 2002 and the recent outbreaks of avian
influenza in Asia are timely reminders of the ever present risks from
respiratory viral diseases. Apart from influenza, there are no vaccines and
very few antiviral chemotherapeutic agents available for the prevention and
treatment of respiratory viral infections-the most common cause of human
illness. If the current H5N1 avian influenza outbreak ever assumes the role of
a pandemic, formidable technical difficulties relating to the properties of the
agent, itself, will ensure that vaccines will only become available after a
significant lead time and then only to a relatively small percentage of the
population. The use of existing antivirals could be critical in limiting the
initial spread of a pandemic, although their use in the control of epidemics
caused by nonpandemic viruses has not been evaluated. It is against this
background that a review of recent developments in respiratory antivirals has been
undertaken. RECENT FINDINGS: The late 1990s were a period of unprecedented
activity in the development of new and much superior antivirals for the
treatment of influenza infections. However, during the past 2 to 3 years and
largely for commercial reasons, there has been a decline in interest in their
further development by major drug companies. This situation may soon change
with the possible advent of new pandemic viruses, and moves are afoot in
several countries to consider the stockpiling of antivirals. The neuraminidase
inhibitors zanamivir and oseltamivir, and the M2 inhibitors amantadine and
rimantadine, remain the only options for controlling respiratory disease caused
by influenza viruses, although the latter two could not be used against very recent
H5N1 strains. There are several other neuraminidase inhibitors in development.
Compounds with activity against other respiratory viruses, notably
rhinoviruses, are also in development, many based on a newer knowledge of viral
protein structure and function (rational drug design). SUMMARY: The following
is an overview of recent papers on the further development of neuraminidase
inhibitors against influenza viruses and on recent development of newer
antivirals against RSV and rhinoviruses. Where possible, comparisons are made
with existing antivirals. For considerations of space, this review has been
structured around stages in the replication cycle of significant respiratory
viruses that have been traditionally used as targets for inhibition.
Descriptors: antiviral agents therapeutic use, respiratory
tract infections drug therapy, respiratory tract infections virology, virus
diseases drug therapy, antiviral agents pharmacology, drugs investigational
pharmacology, drugs investigational therapeutic use, enzyme inhibitors
pharmacology, enzyme inhibitors therapeutic use, ion channels antagonists and
inhibitors.
Brouillette, W.J., S.N. Bajpai, S.M. Ali, S.E. Velu,
V.R. Atigadda, B.S. Lommer, J.B. Finley, M. Luo, and G.M. Air (2003). Pyrrolidinobenzoic
acid inhibitors of influenza virus neuraminidase: Modifications of essential
pyrrolidinone ring substituents. Bioorganic and Medicinal Chemistry
11(13): 2739-2749. ISSN: 0968-0896.
NAL
Call Number: QP550.B55
Abstract: We recently reported the first benzoic acid,
1-(4-carboxy-2-(3-pentylamino)phenyl)-5,5-bis(hydroxymethyl)pyrrolidin-2-one
(8), that is a potent inhibitor of avian influenza A neuraminidase (N9) and,
unlike other reported potent neuraminidase inhibitors, does not contain a basic
aliphatic amine or guanidine nor a simple N-acetyl grouping. However, 8 was a
poor inhibitor of influenza B neuraminidase. In the present study we further
evaluated 8 as an inhibitor of human influenza A NA isolates, and it was
effective against N2 NA but found to be 160-fold less active against N1 NA. We
also synthesized analogues of 8 involving moderate modifications of essential
substituents on the pyrrolidinone ring. Specifically, the aminomethyl (9),
hydroxyethyl (10), and aminoethyl (11) analogues were prepared. Only the most
conservative change (compound 9) resulted in continued effective inhibition of
influenza A, in addition to a noteworthy increase in the activity of 9 for N1
NA. The effectiveness of 9 against influenza B neuraminidase was furthermore
improved 10-fold relative to 8, but this activity remained 50-fold poorer than
for type A NA.
Descriptors: methods and techniques, pharmacology,
influenza, drug therapy, respiratory system disease, viral disease, chemical
synthesis laboratory techniques.
Brown, C.C., H.J. Olander, and D.A. Senne (1992). A
pathogenesis study of highly pathogenic avian influenza virus H5N2 in chickens,
using immunohistochemistry. Journal of Comparative Pathology 107(3):
341-8. ISSN: 0021-9975.
NAL
Call Number: 41.8 J82
Abstract: Eighteen specific pathogen-free chickens
(nine hens older than 1 year and nine 15-week-old males) were inoculated with
highly pathogenic avian influenza virus A/Chicken/Pennsylvania/1370/1983
(H5N2). Birds were serially killed and tissues collected for histological and
immunohistochemical evaluation. In the group of older hens, disease was acute
or peracute. By immunohistochemistry, antigen was abundant in capillary
endothelium in multiple organs, and staining for antigen in parenchymal cells
was marked in brain and heart. In the group of younger male birds, disease was
subacute. Immunohistochemical staining of capillary endothelium was less
pronounced and viral antigen staining was evident in the parenchymal cells of
the heart, brain and kidney.
Descriptors: antigens, viral analysis, brain immunology,
endothelium, vascular immunology, fowl plague pathology, influenza A virus
avian pathogenicity, myocardium immunology, chickens, fowl plague immunology,
immunohistochemistry, avian classification.
Brown, I.H., P.A. Harris, J.W. McCauley, and D.J.
Alexander (1998). Multiple genetic reassortment of avian and human influenza
A viruses in European pigs, resulting in the emergence of an H1N2 virus of
novel genotype. Journal of General Virology 79(Pt. 12):
2947-55. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: Novel H1N2 influenza A viruses which were
first detected in pigs in Great Britain in 1994 were examined antigenically and
genetically to determine their origins and establish the potential mechanisms
for genetic reassortment. The haemagglutinin (HA) of all swine H 1 N2 viruses
examined was most closely related to, but clearly distinguishable both
antigenically and genetically from, the HA of human H1N1 viruses which
circulated in the human population during the early 1 980s. Phylogenetic
analysis of the HA gene revealed that the swine H 1 N2 viruses formed a
distinct branch on the human lineage and were probably introduced to pigs
shortly after 1980. Following apparent transfer to pigs the HA gene underwent
genetic variation resulting in the establishment and cocirculation of
genetically and antigenically heterogeneous virus populations. Genetic analyses
of the other RNA segments of all swine H1N2 viruses indicated that the
neuraminidase gene was most closely related to those of early 'human-like'
swine H3N2 viruses, whilst the RNA segments encoding PB2, PB1, PA, NP, M and NS
were related most closely to those of avian viruses, which have been
circulating recently in pigs in Northern Europe. The potential mechanisms and
probable progenitor strains for genetic reassortment are discussed, but we
propose that the swine H1N2 viruses examined originated following multiple
genetic reassortment, initially involving human H1N1 and 'human-like' swine
H3N2 viruses, followed by reassortment with 'avian-like' swine H1N1 virus.
These findings suggest multiple reassortment and replication of influenza
viruses may occur in pigs many years before their detection as clinical
entities.
Descriptors: influenza A virus avian genetics, human
genetics, recombination, genetic, antigens, viral immunology, base sequence,
DNA, viral, Europe, genes viral, genotype, hemagglutination inhibition tests,
hemagglutinin glycoproteins, influenza virus genetics, avian immunology, human
immunology, molecular sequence data, phylogeny, sequence analysis, DNA, swine.
Brownson, J.M. and B.W. Mahy (1979). Productive
influenza virus infection of synchronized chick embryo fibroblast cells. Journal
of General Virology 42(3): 579-88.
ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The effects of cell metabolic activity on the
outcome of influenza virus infection were studied in partially synchronized
chick embryo fibroblast cultures. There was no evidence to show that the time
in the cell cycle at which cells were infected had any significant effect on
the final virus yield. However, some differences were detected in the length of
the latent period between infections established in synchronized or in
stationary cells. Influenza virus could replicate in synchronized or normal
cell cultures in which DNA synthesis was inhibited with
9-beta-D-arabinofuranosyladenine (ara-A).
Descriptors: influenza A virus avian growth and
development, virus replication drug effects, cell cycle, cell division, chick
embryo, DNA biosynthesis, fibroblasts, avian drug effects, tissue culture,
vidarabine pharmacology.
Brugh, M. and M.L. Perdue (1991). Emergence of
highly pathogenic virus during selective chicken passage of the prototype
mildly pathogenic chicken/Pennsylvania/83 (H5N2) influenza virus. Avian
Diseases 35(4): 824-33. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The prototype mildly pathogenic
A/chicken/Pennsylvania/21525/83 (H5N2) avian influenza virus, which was
isolated more than 5 months before the emergence of highly pathogenic virus in
the major 1983 Pennsylvania outbreak, was examined for the presence of minority
subpopulations of highly pathogenic virus. Selective serial passage of the
parental mildly pathogenic virus in leghorn hens did not lead to recovery of
highly pathogenic virus. However, several highly pathogenic reisolates were
recovered from hens inoculated with either of two mildly pathogenic virus
clones selected for their ability to efficiently produce plaques in trypsin-free
chicken embryo fibroblasts. Unlike the parental virus, these reisolates caused
high mortality in chickens and produced postmortem lesions typical of highly
pathogenic avian influenza. Electrophoretic mobilities of the hemagglutinin
glycoproteins of the highly pathogenic derivatives resembled those of the
prototype highly pathogenic A/chicken/Pennsylvania/1370/83 (H5N2) virus
isolated in October 1983. These results suggest that unrecognized
subpopulations of highly pathogenic virus may have infected Pennsylvania
chickens for several months before emerging as the clinically manifest
component of the virus population.
Descriptors: chickens, fibroblasts microbiology, fowl
plague microbiology, influenza A virus avian pathogenicity, cultured cells,
chick embryo, electrophoresis, polyacrylamide gel, glycoproteins analysis,
hemagglutination inhibition tests, avian chemistry, avian genetics, avian
growth and development, plaque assay, RNA viral analysis, serial passage,
specific pathogen free organisms, viral proteins analysis.
Bruinink, A. and O. Haller (1979). Macrophage
immunity to influenza virus: in vitro and in vivo studies. Experimental Cell Biology 47(3):
190-201. ISSN: 0304-3568.
NAL
Call Number: 448.8 Sch9
Abstract: Using M-TUR, a macrophage-adapted avian
influenza A virus (Hav1, Nav3), antiviral resistance of peritoneal macrophages
obtained from specifically or nonspecifically immunized mice towards in vitro
infection was assessed. M-TUR grew to high titers in macrophages from nonimmune
mice thereby causing a marked cytopathic effect. In contrast, peritoneal
macrophages from mice specifically immunized with TUR virus were not affected
by infection with M-TUR in vitro. This antiviral immunity was specific: mice
immunized with antigenetically unrelated influenza strains such as influenza
A/Hong Kong/1/68 (H3, N2) or influenza B/Lee yielded susceptible macrophages.
Specific macrophage immunity could be abrogated by trypsin treatment in vitro.
Susceptible macrophages from nonimmune hosts became resistant following in
vitro exposure to homologous anti-TUR sera. Peritoneal exudate cells from
BCG-infected animals were less susceptible to in vitro challenge with M-TUR
than control macrophages. In vivo treatment of mice with the unspecific
immunostimulants BCG or Corynebacterium parvum did not protect the animals
against lethal infection with a hepatotropic variant of TUR.
Descriptors: influenza immunology, influenza A virus
immunology, macrophages immunology, antigens, viral, cross reactions, epitopes,
mice, mice inbred c57bl immunology, mice inbred CBA immunology.
Bucher, D.J., I.G. Kharitonenkov, D.K. Lvov, T.V.
Pysina, and H.M. Lee (1980). Comparative study of influenza virus H2 (Asian)
hemagglutinins isolated from human and avian sources. InterVirology
14(2): 69-77. ISSN: 0300-5526.
NAL
Call Number: QR355.I5
Abstract: The hemagglutinin of an influenza virus
isolated from a wild duck (Pintail, Anas acuta) in the USSR in 1976 had
been found to be antigenically indistinguishable from the hemagglutinin of H2N2
viruses of human origin isolated in 1957. The hemagglutinins from viral
preparations of the A/Anas acuta/Primorie/695/76 (H2Nav2) and
A/Singapore/1/57 (H2N2) strains were purified by SDS gel chromatography as the
subunits HA1 and HA2. Comparison of amino acid compositions and peptide maps of
tryptic peptides containing [14C]-carboxymethylcysteine showed a striking
degree of similarity between the H2 hemagglutinins.
Descriptors: hemagglutinins viral analysis, influenza A
virus avian immunology, human immunology, amino acids analysis, ducks
microbiology, peptides analysis.
Buckler White, A.J. and B.R. Murphy (1986). Nucleotide sequence analysis of the
nucleoprotein gene of an avian and a human influenza virus strain identifies
two classes of nucleoproteins. Virology 155(2): 345-55. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The nucleotide sequences of RNA segment 5 of
an avian influenza A virus, A/Mallard/NY/6750/78 (H2N2), and a human influenza
A virus, A/Udorn/307/72 (H3N2), were determined and the deduced amino acid
sequences of the nucleoprotein (NP) of these viruses were compared to two other
avian and two other human influenza A NP sequences. The results indicated that
there are separate classes of avian and human influenza A NP genes that can be
distinguished on the basis of sites containing amino acids specific for avian
and human influenza viruses and also by amino acid composition. The human
influenza A virus NP genes appear to follow a linear pathway of evolution with
the greatest homology (96.9%) between A/NT/60/68 (H3N2) and A/Udorn/72,
isolated only 4 years apart, and the least homology (91.1%) between A/PR/8/34
(H1N1) and A/Udorn/72, isolated 38 years apart. Furthermore, 84% of the
nucleotide substitutions between A/PR/8/34 and A/NT/60/68 are preserved in the
NP gene of the A/Udorn/72 strain. In contrast, a distinct linear pathway is not
present in the avian influenza NP genes since the homology (90.3%) between the
two avian influenza viruses A/Parrot/Ulster/73 (H7N1) and A/Mallard/78 isolated
only 5 years apart is not significantly greater than the homology (90.1%)
between strains A/FPV/Rostock/34 and A/Mallard/78 isolated 44 years apart and
only 49% of the nucleotide substitutions between A/FPV/34 and A/Parrot/73 are found
in A/Mallard/78. A determination of the rate of evolution of the human
influenza A virus NP genes suggested that there were a greater number of
nucleotide substitutions per year during the first several years immediately
following the emergence of a new subtype in 1968.
Descriptors: influenza A virus genetics, nucleoproteins
genetics, viral proteins genetics, amino acid sequence, base sequence,
evolution, genes viral, nucleoproteins classification, RNA viral genetics,
sequence homology, nucleic acid, viral proteins classification.
Buckler White, A.J., C.W. Naeve, and B.R. Murphy
(1986). Characterization of a gene coding for M proteins which is involved
in host range restriction of an avian influenza A virus in monkeys. Journal
of Virology 57(2): 697-700. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: The nucleotide sequence of the region of RNA
segment 7 coding for the M1 and M2 proteins of avian influenza A/Mallard/New
York/6750/78 was determined, and the deduced amino acid sequences were compared
to other avian and human M protein sequences. The M2 proteins of the avian and
human viruses have diverged much more than the M1 proteins, although amino
acids specific for avian and human viruses were found in both M1 and M2
proteins.
Descriptors: genes viral, influenza A virus avian genetics,
RNA viral genetics, viral proteins genetics, amino acid sequence, haplorhini
microbiology, avian growth and development, messenger genetics.
Bukrinskaia, A.G. and T.A. Asadullaev (1968). Sravnitel'noe
deistvie gistonov i 6-azauridina na reproduktsiiu miksovirusov. [Comparative
effect of histones and 6-azauridine on the reproduction of myxoviruses]. Voprosy
Virusologii 13(5): 549-54. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: histones pharmacology, orthomyxoviridae drug
effects, triazines pharmacology, virus replication drug effects, influenza A
virus avian drug effects, Newcastle disease virus drug effects, RNA viral
antagonists and inhibitors.
Bukrinskaia, A.G., G.V. Kornilaeva, N.K. Vorkunova,
N.G. Timofeeva, and G.I. Shaposhnikova (1982). Gangliozidy--spetsificheskie
retseptory dlia virusa grippa. [Gangliosides--specific receptors for the
influenza virus]. Voprosy Virusologii 27(6): 661-6. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The capacity of two gangliosides, GD1a and
GT1b isolated from bovine brain to function as specific receptors of influenza
virus was determined. A primary chick fibroblast culture was treated with
neuraminidase to destroy natural receptors, the cells were loaded with
gangliosides GD1a and GT1b, inoculated with 3H-uridine-labeled virus, and virus
adsorption and penetration into the cell nucleus were determined. Both
gangliosides were shown to restore virus adsorption to the cell surface and
penetration of viral structures into the cell, GT1b facilitating more effective
transportation of viral structures into the nuclei than GD1a and inducing
penetration into the nuclei nearly 1.5-fold as much amount of viral structures
as in native cells. The same ganglioside partially restored virus-induced
hemolysis upon loading it on erythrocytes pre-treated with neuraminidase. It is
concluded that ganglioside GT1b is a specific receptor for influenza virus.
3.9% of this ganglioside was found in chick fibroblast lipids.
Descriptors: gangliosides metabolism, orthomyxoviridae
metabolism, receptors, virus metabolism, adsorption, cell nucleus metabolism,
chick embryo, erythrocytes metabolism, fibroblasts metabolism, hemolysis,
influenza A virus avian metabolism.
Bukrinskaia, A.G., N.V. Prokazova, G.I.
Shaposhnikova, S.L. Kocharov, and S.L. Shevchenko (1982). Rol' gangliozidov
v retseptsii i proniknovenii v kletku virusa grippa. [Role of gangliosides in
influenza virus reception and penetration into the cell]. Doklady Akademii
Nauk SSSR 263(6): 1481-4. ISSN:
0002-3264.
NAL
Call Number: 511 P444A
Descriptors: cell transformation, viral drug effects,
gangliosides pharmacology, influenza A virus avian pathogenicity, receptors,
virus drug effects, adsorption, carcinoma, Ehrlich tumor microbiology, avian
drug effects, neuraminidase pharmacology.
Bukrinskaya, A.G., A.K. Gitelman, and V.B. Martynenko
(1978). Abortive infection of influenza virus in Ehrlich ascites tumor
cells. Unusual fragility of virus particles. Archives of Virology
56(4): 279-90. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Noninfectious virus particles were produced
in Ehrlich ascites tumor cells infected intraperitoneally with fowl plague
virus. The PFU yield of virus per cell was less than 0.1 and the ratio PFU/HA
units in the progeny virus was less than 10(3). The virus particles had the
same morphology and size as egg-grown virus but were more fragile. They were
disrupted by centrifugation through sucrose and caesium chloride gradients, but
this disruption was avoided by fixing the particles with formaldehyde before
centrifugation. Analysis of polypeptides by SDS-PAGE showed that ascites-grown
virus particles contained reduced amounts of matrix protein compared with
egg-grown virus.
Descriptors: carcinoma, Ehrlich tumor microbiology,
influenza A virus avian growth and development, centrifugation, density
gradient, avian enzymology, avian ultrastructure, mice, neoplasm
transplantation, neuraminidase metabolism, peptides analysis, viral proteins
analysis, virus replication.
Bukrinskaya, A.G., A.K. Gitelman, V.B. Martynenko,
and T.A. Assadulaev (1979). Properties of influenza virus nucleocapsids in
nonpermissive cells. Acta Virologica 23(5): 353-9. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: The properties of fowl plague virus
(influenza virus A) nucleocapsids isolated from the cytoplasm of infected
Ehrlich ascites carcinoma cells and chick embryo cells were compared. Nucleocapsids
isolated from both systems possessed similar polypeptides (P and NP) but
differed in their biophysical characteristics. Nucleocapsids from ascites cells
sedimented in velocity sucrose gradients slower (from 25 to 50 S) and the
majority of them banded at higher density in CsCl gradients (rho 1.38 as
compared to 1.34 g/ml) than nucleocapsids from chick embryo cells. In the
electron microscope they appeared as thin threads 3--4 nm in diameter.
Descriptors: capsid analysis, influenza A virus avian analysis,
viral proteins analysis, capsid biosynthesis, carcinoma, Ehrlich tumor,
cultured cells, centrifugation, density gradient, chick embryo, cytoplasm
analysis, avian growth and development, avian metabolism, mice, microscopy,
electron.
Bullough, P.A. and P.A. Tulloch (1991). Spot-scan
imaging of microcrystals of an influenza neuraminidase-antibody fragment
complex. Ultramicroscopy 35(2): 131-43.
ISSN: 0304-3991.
NAL
Call Number: QH201.U4
Abstract: Electron micrographs of two-dimensional
microcrystals of a complex of an avian influenza virus neuraminidase and an
antibody Fab fragment, termed 32/3, have been recorded using the spot-scan
method of imaging. The crystals have a large unit cell (159.5 A x 159.5 A x
130.5 A) and a high solvent content (approximately 71% by volume) and are a
challenging specimen for testing the spot-scan methodology. Crystalline order
was preserved to beyond 4 A resolution as demonstrated by electron diffraction,
using an embedding medium of a mixture of glucose and neutral potassium
phosphotungstate. Using a Philips C400 computer control system interfaced to an
EM420 electron microscope, and with the inclusion of additional software in the
system, we have been able to record micrographs at low temperature with a
relatively narrow (1500 A diameter) moving beam. There is evidence that the use
of such a spot-scan beam reduces the effects of beam-induced specimen motion on
the quality of micrographs. Conventional low-dose "flood-beam" images
showed good isotropic optical diffraction in only 15% of cases whereas 30% of
spot-scan images showed good diffraction. The best flood-beam images gave
phases to only 15 A resolution after computer processing, whereas the best
spot-scan images gave phases to 7 A resolution. Electron diffraction patterns
were also recorded at low temperature, and the resulting diffraction amplitudes
combined with phases from spot-scan images to yield a projection map of the
structure. A 7 A resolution projection map of the complex is presented, and is
compared with the projection map of the same avian influenza neuraminidase
complexed with a different monoclonal Fab fragment, NC41, which has been solved
to high resolution by X-ray diffraction.
Descriptors: antibodies, viral chemistry, image
processing, computer assisted, immunoglobulins, Fab ultrastructure, influenza A
virus avian ultrastructure, neuraminidase ultrastructure, binding sites,
crystallization, crystallography, immunoglobulins, Fab chemistry, avian
enzymology, avian immunology, microscopy, electron, neuraminidase chemistry,
x-ray diffraction.
Burger, H., H. Steuler, and C. Scholtissek (1985). A
mutant of fowl plague virus (influenza A) with an enhanced electrophoretic
mobility of RNA segment 8. Journal of General Virology 66(Pt. 8):
1679-86. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: A temperature-sensitive mutant (ts 1/9)
obtained by undiluted passage of fowl plague virus (FPV) at 33 degrees C
carried a strong ts defect in RNA segment 6 [neuraminidase (NA) gene] and a
weak ts defect in RNA segment 8 [non-structural (NS) protein Although the viral
proteins have normal migration rates, the NS gene migrated during
polyacrylamide gel electrophoresis (PAGE) significantly faster than the NS gene
of wild-type FPV, even after denaturation by glyoxal. Despite this observation,
the NS gene of ts 1/9 did not carry a deletion as shown by sequence
determination. There were only five base replacements which resulted in three
changes in amino acids. Three of the base replacements led to a more compact
secondary structure of RNA segment 8, which seems to be responsible for the
faster migration rate during PAGE and which seems to resist, at least
partially, the treatment with glyoxal.
Descriptors: influenza A virus avian genetics, mutation,
RNA viral isolation and purification, amino acid sequence, base sequence,
cultured cells, chick embryo, cloning, molecular, genes, structural, genes
viral, hemagglutinins genetics, neuraminidase genetics, plasmids, viral
genetics, RNA directed DNA polymerase metabolism.
Bush, R.M. (2004). Influenza as a model system for
studying the cross-species transfer and evolution of the SARS coronavirus. Philosophical
Transactions of the Royal Society of London. Series B Biological Sciences
359(1447): 1067-73. ISSN: 0962-8436.
NAL
Call Number: 501 L84Pb
Abstract: Severe acute respiratory syndrome coronavirus
(SARS-CoV) moved into humans from a reservoir species and subsequently caused
an epidemic in its new host. We know little about the processes that allowed
the cross-species transfer of this previously unknown virus. I discuss what we
have learned about the movement of viruses into humans from studies of
influenza A, both how it crossed from birds to humans and how it subsequently
evolved within the human population. Starting with a brief review of severe
acute respiratory syndrome to highlight the kinds of problems we face in
learning about this viral disease, I then turn to influenza A, focusing on
three topics. First, I present a reanalysis of data used to test the hypothesis
that swine served as a "mixing vessel" or intermediate host in the
transmission of avian influenza to humans during the 1918 "Spanish
flu" pandemic. Second, I review studies of archived viruses from the three
recent influenza pandemics. Third, I discuss current limitations in using
molecular data to study the evolution of infectious disease. Although influenza
A and SARS-CoV differ in many ways, our knowledge of influenza A may provide
important clues about what limits or favours cross-species transfers and
subsequent epidemics of newly emerging pathogens.
Descriptors: evolution, molecular, influenza transmission,
influenza A virus physiology, models, biological, phylogeny, SARS virus
physiology, zoonoses virology, influenza genetics, influenza A virus genetics,
swine virology.
Cabezas, J.A. (1991). Etudes sur la sialidase et
l'esterase des virus de la grippe. [Studies on sialidase and esterase in
influenza viruses]. Annales Pharmaceutiques Francaises 49(2):
57-66. ISSN: 0003-4509.
NAL
Call Number: 396.8 AN7
Abstract: The main contributions of the author and
collaborators about sialidase (EC 3.2.1.18) of influenza virus types A and B
and O-acetylesterase (EC 3.1.1.53) of type C are summarized. After a short
introduction on the topic, the negative results obtained by the author on
inhibitors are commented. Then, the peculiarities of the three procedures
assayed, based on the NADH determination as a measurement for the sialidase
activity, are discussed. The spectrofluorimetric measurement of NADH concentration
is a more sensitive and convenient procedure than that by spectrophotometry,
although it is less sensitive than that based on bioluminiscence. Sialidase
activity is generally higher in influenza virus type A than in type B; however,
some differences have been found between the three sub-types A analysed.
Furthermore, thermal stability and stability against changes in the pH values
are higher for influenza virus from ducks, followed by those from humans and,
finally, by those from pigs. O-acetylesterase of influenza virus type C shows a
broad specificity; it acts on O-acetyl-containing compounds which may not be
sialic acids. It seems that this enzyme might contribute to facilitate the
action of sialidase of influenza virus types A and B. The peculiarities of
influenza virus type C suggest to include this type as a new genus in the
future classification of viruses.
Descriptors: carboxylic ester hydrolases analysis,
neuraminidase analysis, orthomyxoviridae enzymology, ducks, fowl plague
enzymology, influenza enzymology, influenza A virus avian enzymology, human
enzymology, porcine enzymology, influenza B virus enzymology, influenza virus C
enzymology, orthomyxoviridae infections enzymology, swine.
Cameron, K.R., V. Gregory, J. Banks, I.H. Brown, D.J.
Alexander, A.J. Hay, and Y.P. Lin (2000). H9N2 subtype influenza A viruses
in poultry in Pakistan are closely related to the H9N2 viruses responsible for
human infection in Hong Kong. Virology 278(1): 36-41. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: disease outbreaks veterinary, influenza
veterinary, influenza A virus avian classification, human classification,
poultry diseases virology, antigens, viral genetics, antigens, viral immunology,
cloning, molecular, genome, viral, hemagglutination inhibition tests,
hemagglutinins viral genetics, Hong Kong epidemiology, influenza epidemiology,
avian genetics, avian immunology, human genetics, human immunology, molecular
sequence data, Pakistan epidemiology, phylogeny, poultry diseases epidemiology,
sequence analysis, protein, viral proteins genetics, viral proteins immunology.
Capua, I., F. Mutinelli, and M.H. Hablovarid (2002). Avian
embryo susceptibility to Italian H7N1 avian influenza viruses belonging to
different genetic lineages. Archives of Virology 147(8): 1611-21. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: In the present paper we report of the results
of an immunohistochemical investigation to assess tissue tropism and viral
replication in developing chicken, turkey, Muscovy duck and mallard duck
embryos, of Italian H7N1 isolates belonging to different genetic lineages. LPAI
isolates were chosen on the basis of the location in the phylogenetic tree: a
progenitor strain, A/ty/Italy/977/V99, (exhibiting no additional glycosylation
site, nAGS), strain A/ty/Italy/2379/V99 (AGS in position 123) and strain
A/ty/Italy/3675/V99 (AGS in position 149) were selected. The latter two strains
belonged to distinct lineages originating from the pool of progenitor strains.
HPAI isolate A/ty/Italy/4580/V99 was also included in the study. All the
embryos tested supported the growth of HPAI. The LPAI isolates replicated
readily in the allantoic layer of the CAM of all the species tested, and did
not grow in the developing chicken, turkey and Muscovy duck embryos. In
contrast, they replicated to different extents in the respiratory tract of the
developing mallard embryo, which also presented lower mortality rates than the
other species. We conclude from these findings that the pathogenesis of LPAI
infections in mallard embryos is different to that observed in other species,
and should be investigated further.
Descriptors: allantois virology, chick embryo virology,
chorion virology, influenza A virus avian pathogenicity, disease
susceptibility, ducks, embryo loss etiology, glycosylation, immunohistochemistry, avian genetics,
turkeys.
Capua, I., C. Terregino, G. Cattoli, and A. Toffan
(2004). Increased resistance of vaccinated turkeys to experimental infection
with an H7N3 low-pathogenicity avian influenza virus. Avian Pathology
33(2): 158-163. ISSN: 0307-9457.
NAL
Call Number: SF995.A1A9
Descriptors: avian influenza virus, disease control,
disease prevention, disease resistance, experimental infection, immune
response, vaccination, turkeys.
Caric Lazar, M., C. Scholtissek, and R. Rott (1975). Effect
of tetraethyl thiuram disulfide (disulfiram) on the multiplication of enveloped
viruses. Archives of Virology 48(4): 297-306. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Disulfiram at concentrations between 0.1 and
0.3 mM inhibits the multiplication of Semliki Forest virus (SFV), fowl plague
virus (FPV), Newcastle disease virus (NDV), vesicular stomatitis virus (VSV),
and pseudorabies virus (PRV), when administered 1 hour before and during
adsorption. There is, however, no inhibition of virus multiplication, when the
drug is added after adsorption onto chick embryo cells. Disulfiram interferes
neither with the receptors of the virus nor of erythrocytes, and it does not
prevent virus adsorption. Possibly an early step in virus multiplication is
affected by disculfiram. Infected cells once treated with the drug recover
after some time of incubation in an ingibitor-free medium. The inhibitory state
can be maintained, however, if relatively low doses of disulfiram are present
in the culture medium also after adsorption. Disulfiram has no effect on
macromolecular synthesis of the host cells. It has, however, a marked affect on
membrane function. While virus multiplication is readily inhibited by
disulfiram when chick embryo or BHK cells were investigated, virus
multiplication in HeLa cells is almost resestant against the action of
disulfiram.
Descriptors: disulfiram pharmacology, herpesviridae growth
and development, herpesvirus 1, suid growth and development, influenza A virus
avian growth and development, Newcastle disease virus growth and development,
Semliki Forest virus growth and development, vesicular stomatitis Indiana virus
growth and development, virus replication drug effects, adsorption, ditiocarb
pharmacology, erythrocytes drug effects, ethanol pharmacology, influenza A
virus avian drug effects, Newcastle disease virus drug effects, pseudorabies
drug therapy, Semliki Forest virus drug effects, tissue culture, vesicular
stomatitis Indiana virus drug effects.
Carroll, S.M. and J.C. Paulson (1985). Differential
infection of receptor-modified host cells by receptor-specific influenza
viruses. Virus Research 3(2): 165-79. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Influenza viruses of contrasting receptor
specificity have been examined for their ability to infect receptor-modified
MDCK cells containing sialyloligosaccharide receptor determinants of defined
sequence. Cells were treated with sialidase to remove sialic acid and render
them resistant to infection and were then incubated with sialyltransferase and
CMP-sialic acid to restore sialic acid in the SA alpha 2,6Gal or SA alpha
2,3Gal linkages. The viruses A/RI/5 + /57 and A/duck/Ukraine/1/63, previously
shown to exhibit preferential binding of SA alpha 2,6Gal and SA alpha 2,3Gal
linkages, respectively, were found to exhibit differential infection of the
receptor-modified cells in accord with their receptor specificity. Coinfection
of SA alpha 2,3Gal derivatized cells with a mixture of the two viruses resulted
in selective propagation of the SA alpha 2,3Gal-specific A/duck/Ukraine/1/63
virus. The results demonstrate the potential for cell surface receptors to
mediate selection of receptor-specific variants of influenza virus.
Descriptors: influenza A virus avian metabolism, human
metabolism, oligosaccharides metabolism, receptors, virus metabolism,
adsorption, antibodies, viral analysis, binding sites, cell line, dogs,
erythrocytes microbiology, hemagglutinins viral, avian immunology, human
immunology, kidney, neuraminidase metabolism, receptors, virus genetics,
receptors, virus immunology, sialic acids metabolism, sialyltransferases
metabolism, species specificity, viral proteins analysis.
Carter, M.J. and B.W. Mahy (1982). Incomplete
avian influenza A virus displays anomalous interference. Archives of
Virology 74(1): 71-6. ISSN:
0304-8608.
NAL
Call Number: 448.3 Ar23
Descriptors: influenza A virus avian physiology, viral
interference, cultured cells, chick embryo, defective viruses physiology,
fibroblasts, kinetics, probability.
Carter, M.J. and B.W. Mahy (1982). Synthesis of
RNA segments 1-3 during generation of incomplete influenza A (fowl plague)
virus. Archives of Virology 73(2): 109-19. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: Incomplete influenza A virus (fowl plague
Dobson strain) was prepared by undiluted passage in primary chick embryo
fibroblast cells. Analysis of released virus RNA revealed a deficiency in RNA
segments 1-3, characteristic of incomplete virus formation. The virus yield
from a high multiplicity infection with standard virus always showed this
deficiency, even when analysed as early as 6 hours post-infection, whereas infection
at low multiplicity gave rise to virus indistinguishable in RNA composition
from the parent virus. The relative amounts of intracellular,
non-polyadenylated, complementary RNA (template RNA) were found to reflect
accurately the eventual RNA composition of released virus, and were altered in
phase with PFU:HAU ratio, throughout a von Magnus cycle.
Descriptors: defective viruses growth and development,
influenza A virus avian growth and development, RNA viral biosynthesis,
cultured cells, chick embryo, defective viruses metabolism, avian metabolism,
kinetics, plaque assay, templates, genetic.
Caton, A.J. and J.S. Robertson (1980). Structure
of the host-derived sequences present at the 5' ends of influenza virus mRNA.
Nucleic Acids Research 8(12): 2591-603.
ISSN: 0305-1048.
NAL
Call Number: QD341.A2N8
Abstract: Nucleotide sequence analysis of the terminal
virus-coded regions of a clone of the matrix gene of influenza virus indicated
that the region corresponding to the 5' end of the mRNA contains an additional
13 non-virus coded nucleotides. Using the dideoxy-chain termination sequencing
method with a restriction fragment derived from this clone, we have determined
that the 5' ends of matrix gene mRNAs contain a heterogenous sequence of 9-15
nucleotides. In addition, the data indicate that the 3' terminal nucleotide of
matrix gene virion RNA is not transcribed into mRNA, transcription of influenza
virus-specific sequences commencing with the penultimate nucleotide at the 3'
end of viron RNA.
Descriptors: influenza A virus avian analysis, RNA,
messenger, viral, base sequence, cloning, molecular, DNA restriction enzymes,
DNA, recombinant.
Cattoli, G., V. Brasola, and I. Capua (2003). Plaque
morphology of Italian H7N1 LPAI isolates in MDCK cells and in primary cells of
different avian species. Avian Diseases 47(Special Issue):
1161-1163. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The morphology of plaques induced by Italian,
H7N1, low-pathogenic avian influenza (LPAI) viruses belonging to different
lineages was investigated in primary chicken, turkey, Muscovy duck, and mallard
duck kidney cells and in MDCK cells in the absence of trypsin. LPAI isolates
were selected on the basis of the location in the phylogenetic tree: 977/V99
(located at the root, no additional glycosylation site (nAGS)), 2379/V99 (AGS
in position 123), and 3675/V99 (AGS in position 149). Different isolates did
not induce plaques with a statistically significant different size in MDCK
cells. However, in primary cells of different avian origin, the presence or
absence of AGS significantly influenced plaque size. Generally speaking,
977/V99 was the least efficient at plaquing in all cells, while 2379/V99 (AGS
in position 123) plaqued more efficiently in turkey cells and 3675/V99 (AGS in
position 149) in chicken cells. The presence of either AGS induced
statistically significant larger plaques in cells of waterfowl origin.
Descriptors: cell biology, infection, avian influenza,
infectious disease, respiratory system disease, viral disease, cell culture
culturing techniques, laboratory techniques, glycosylation sites plaque
morphology.
Chambers, T.M. and R.G. Webster (1987). Defective
interfering virus associated with A/Chicken/Pennsylvania/83 influenza virus.
Journal of Virology 61(5): 1517-23.
ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: The A/Chicken/Pennsylvania/1/83 influenza
virus, isolated from a respiratory infection of chickens, is an avirulent H5N2
virus containing subgenomic RNAs (W.J. Bean, Y. Kawaoka, J.M. Wood, J.E.
Pearson, and R.G. Webster, J. Virol. 54:151-160, 1985). We show here that
defective interfering particles are present in this virus population. The virus
had a low ratio of plaque-forming to hemagglutinating units and produced
interference with standard virus multiplication in infectious center reduction
assays. Subgenomic RNAs were identified as internally deleted polymerase RNAs.
We have confirmed that this virus protects chickens from lethal H5N2 influenza
virus infection. This protective effect appeared to be due to the inhibition of
virulent virus multiplication. Additionally, subgenomic RNAs derived from
polymerase RNAs were detected in 5 of 18 RNA preparations from animal influenza
virus isolates. Therefore, defective interfering particles are sometimes
produced in natural influenza virus infections, not just under laboratory
conditions. These particles may be capable of suppressing the pathogenic effect
of virulent virus infections in nature.
Descriptors: defective viruses genetics, influenza A virus
avian genetics, DNA directed RNA polymerases genetics, defective viruses growth
and development, genes viral, avian growth and development, viral genetics,
viral interference, virus replication.
Chambers, T.M., S. Yamnikova, Y. Kawaoka, D.K. Lvov,
and R.G. Webster (1989). Antigenic and molecular characterization of subtype
H13 hemagglutinin of influenza virus. Virology 172(1): 180-8. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Influenza A viruses with subtype H13
hemagglutinin display an unusual host range. Although common in shorebirds,
they are very rare or absent in wild ducks; additionally, H13 viruses have been
isolated from a whale. To study the molecular basis for this host range, we
have determined the complete nucleotide sequences of the hemagglutinin genes of
three H13 influenza viruses from different species or geographical areas:
A/gull/Maryland/77, A/gull/Astrachan (USSR)/84, and A/pilot whale/Maine/84.
Based on the deduced amino acid sequences, H13 hemagglutinin shares the basic
structure of other type A hemagglutinin subtypes such as H3, but has clearly
diverged from other completely sequenced subtypes. Unique features of H13
hemagglutinin include the occurrence, near the receptor binding pocket, of
residues Arg/Lys-227 and Trp-229 (H3 numbering); the significance of these are
unknown. The sequence of the HA1-HA2 cleavage site resembles those of avirulent
avian influenza viruses. The whale H13 hemagglutinin is similar to those from
gulls, supporting the hypothesis that influenza viruses from avian sources can
enter marine mammal populations but are probably not permanently maintained
there. Antigenic analysis using a panel of monoclonal antibodies suggests that,
like other subtypes, H13 viruses are heterogeneous, with different antigenic
variants predominating in the eastern versus the western hemispheres.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, amino acid sequence, base sequence, genes viral,
hemagglutinins viral classification, hemagglutinins viral genetics, avian
classification, influenza A virus avian genetics, molecular sequence data, RNA
viral genetics.
Chen Hualan, Yu Kangzhen, and Tian Guobin (1997). Amplification
and cloning of haemagglutinin genes of avian influenza virus of H5 and H7
subtypes by RT-PCR. Chinese Journal of Animal and Poultry Infectious
Diseases (2): 16-18. ISSN:
1001-6961.
Descriptors: poultry, avian influenza virus, DNA, nucleotide
sequence, molecular cloning, acids, domestic animals, genetic engineering,
genomes, influenza virus, livestock, nucleic acids, nucleic compounds, organic
acids, orthomyxoviridae, useful animals, viruses.
Chepulis, G.K., A.F. Bocharov, and V.M. Zhdanov (1967).
Ionoobmennaia khromatografiia virusa klassicheskoi chumy ptits na
tselliuloznykh obmennikakh. [Ion-exchange chromatography of classical fowl
plague virus on cellulose exchangers]. Voprosy Virusologii 12(4):
439-45. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian isolation and
purification, cellulose, chromatography, ion exchange.
Chepulis, G.K. and V.M. Zhdanov (1970). Cellular
antigens in myxo- and paramyxoviruses as revealed by immunodiffusion methods.
Experientia 26(10): 1141-3. ISSN: 0014-4754.
NAL
Call Number: 475 Ex7
Descriptors: abo blood group system analysis, antigens
analysis, erythrocytes immunology, fetal membranes immunology, haptens
analysis, immunodiffusion, immunoelectrophoresis, influenza A virus avian
immunology, kidney immunology, Newcastle disease virus immunology,
parainfluenza virus 1, human immunology, guinea pigs, immunity, cellular,
methods, rabbits, rats.
Chepulis, G.S., I.U.S. Derkach, and V.M. Zhdanov
(1972). Belkovye komponenty virusa klassicheskoi chumy ptits i virusa
bolezni N'iukasla. [Protein components of classical fowl plague virus and
Newcastle disease virus]. Voprosy Virusologii 17(1): 48-52. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: influenza A virus avian analysis, Newcastle
disease virus analysis, viral proteins analysis, antigens, viral analysis,
centrifugation, density gradient, electrophoresis, disc, immunodiffusion.
Chepulis, G.S., V.M. Zhdanov, I. Nas, I. Cherba, and
K. Rozha (1971). Vyiavlenie kletochnykh antigenov u miksovirusov i
paramiksovirusov metodami immunodiffuzii. [Detection of cellular antigens in
myxoviruses and paramyxoviruses by the immunodiffusion method]. Voprosy
Virusologii 16(1): 62-70. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antigens analysis, influenza A virus avian
immunology, Newcastle disease virus immunology, orthomyxoviridae immunology,
parainfluenza virus 1, human immunology, antigens, viral analysis, guinea pigs,
immunodiffusion, immunoelectrophoresis, rabbits, rats, species specificity.
Cherednichenko, O.G., Z.M. Biiasheva, and N.B.
Akhmatullina (2001). Geneticheskii analiz retsessivnykh letal'nykh mutatsii,
indutsirovannykh virusom grippa v X-khromosome Drosophila melanogaster.
[Genetic analysis of recessive lethal mutations induced by the influenza virus
in the X chromosome of Drosophila melanogaster]. Genetika 37(7): 908-14.
ISSN: 0016-6758.
NAL
Call Number: QH431.A1G4
Abstract: Mutagenic potential of the influenza virus
was evaluated. Based on its capacity of inducing recessive lethal mutations in
the X chromosome of Drosophila
melanogaster, the influenza virus can be classified as a moderate-activity
mutagen. Its mutagenicity does not depend on ability to reproduce in the cell system.
This virus was shown to disrupt formation of the wing, particularly wing vein
M1 + 2. Cytogenetic examination of polytene X chromosomes bearing recessive
lethal mutations in Drosophila salivary glands did not reveal chromosome
rearrangements. These lethals are assumed to be small deletions or point
mutations. The determination of the lethal activity stage of these mutations
showed that they disrupt the expression of genes functioning at various
developmental stage of Drosophila. Two of them were conditionally lethal
(temperature-sensitive). Two of 15 mutations analyzed were mapped to region
2B9-10-3C10-11.
Descriptors: Drosophila melanogaster genetics, Drosophila
melanogaster virology, influenza A virus avian genetics, mutagenesis, X
chromosome genetics, genes, lethal, genes, recessive, point mutation.
Chiu, S.Y., H.K. Shieh, J.H. Shien, S.Y. Tai, and
L.H. Lee (1994). Preparation of monoclonal antibody against avian influenza
virus H5N9 strain. Journal of the Chinese Society of Veterinary Science
20(1): 40-50. ISSN: 0253-9179.
NAL
Call Number: SF604.C54
Abstract: The spleen of BALB/c mice, which had been
immunized five times with purified avian influenza virus, H5N9 strain, and had
good antibody response, was harvested; the spleen cells were fused with NS-1
myeloma cells. After a screening for specific antibody production with the
ELISA test, 18 of 460 wells showed strong positive reactions. Three further
subclonings established nine strains of hybridoma with stable activities of
secreting monoclonal antibodies. The isotypes of the nine monoclonal antibodies
were all IgG1, and all their light chains also belong to the kappa chain. The
antibodies were applied on CEF cultures infected with AIV H5N9 by means of
indirect fluorescent antibody staining. Fluorescence was observed among the
cell cytoplasm only. All monoclonal antibodies had HI and neutralization
abilities, but formed no precipitation line in a immunodiffusion test. One
antibody reacted with viral polypeptide, which was HA2 antigen with molar mass
28 kD, according to the western blotting test. In order to detect the
specificity, we reacted the monoclonal antibody with AIV subtypes H1 through
H12, respectively, according to the HI test. Besides H5N9, the antibody reacted
with strain H8N4, but not H8N6. Viral protein analysis by means of SDS-PAGE
revealed that both H5N9 and H8N4 had common peptide bands 69, 57, 48, 37 and 28
kD, especially the peptide of HA2, 28 kD.
Descriptors: immune system, infection, microbiology, pathology,
pharmacology, veterinary medicine, vaccination viral protein analysis.
Chizhov, N.P. (1974). Protivovirusnoe deistvie
nukleaz i gistonov [Antiviral action of nucleases and histones]. Voprosy
Virusologii (6): 647-52. ISSN:
0507-4088.
NAL
Call Number: 448.8 P942
Descriptors: antiviral agents pharmacology,
deoxyribonucleases pharmacology, histones pharmacology, ribonucleases
pharmacology, adenoviridae drug effects, adenoviridae infections drug therapy,
antiviral agents therapeutic use, aphthovirus drug effects, conjunctivitis drug
therapy, DNA, viral biosynthesis, deoxyribonucleases therapeutic use,
encephalitis virus, Venezuelan equine drug effects, encephalitis viruses, tick
borne drug effects, herpesviridae infections drug therapy, histones therapeutic
use, influenza A virus avian drug effects, keratitis, dendritic drug therapy,
meningitis, viral drug therapy, Newcastle disease virus drug effects,
orthomyxoviridae drug effects, polioviruses drug effects, RNA viral
biosynthesis, ribonucleases therapeutic use, simplexvirus drug effects,
vaccinia virus drug effects, vesicular stomatitis Indiana virus drug effects,
virus replication drug effects.
Choi, Y.K., S.M. Goyal, M.W. Farnham, and H.S. Joo
(2002). Phylogenetic analysis of H1N2 isolates of influenza A virus from
pigs in the United States. Virus Research 87(2): 173-9. ISSN: 0168-1702.
NAL
Call Number: QR375.V6
Abstract: Twenty-four H1N2 influenza A viruses were
newly isolated from pigs in the United States. These isolates originated from
19 farms in 9 different swine producing states between 1999 and 2001. All farms
had clinical histories of respiratory problem and/or abortion. The viral
isolates were characterized genetically to determine the origin of all eight
gene segments. The results showed that all H1N2 isolates were reassortants of
classical swine H1N1 and triple reassortant H3N2 viruses. The neuraminidase
(NA) and PB1 genes of the H1N2 isolates were of human origin, while the
hemagglutinin (HA), nucleoprotein (NP), matrix (M), non-structural (NS), PA and
PB2 polymerase genes were of avian or swine origin. Fifteen of the 24 H1N2
isolates were shown to have a close phylogenic relationship and high amino acid
homology with the first US isolate of H1N2 (A/SW/IN/9K035/99). The remaining nine
isolates had a close phylogenic relationship with classical swine influenza
H1N1 in the HA gene. All other genes including NA, M, NP, NS, PA, PB1 and PB2
showed a close phylogenic relationship with the H1N2 (A/SW/IN/9K035/99) strain
and triple reassortant H3N2 viruses. However, PB1 genes of two isolates
(A/SW/KS/13481-S/00, A/SW/KS/13481-T/00) were originated from avian influenza A
virus lineage. These results suggest that although there are some variations in
the HA genes, the H1N2 viruses prevalent in the US swine population are of a
similar genetic lineage.
Descriptors: influenza A virus, porcine genetics,
antigens, viral, hemagglutinin glycoproteins, influenza virus genetics, porcine
classification, porcine enzymology, porcine isolation and purification,
molecular sequence data, neuraminidase
genetics, phylogeny, swine, United States, variation genetics.
Chucholowius, H.W. and R. Rott (1972). A new
method for purification of myxoviruses by zonal centrifugation with two
different sucrose density gradients. Proceedings of the Society for
Experimental Biology and Medicine, New York, NY 140(1): 245-7. ISSN: 0037-9727.
NAL
Call Number: 442.9 So1
Descriptors: orthomyxoviridae isolation and purification,
centrifugation, density gradient, centrifugation, zonal, influenza A virus
avian isolation and purification, methods, Newcastle disease virus isolation
and purification, sucrose.
Ciampor, F., P.M. Bayley, M.V. Nermut, E.M. Hirst,
R.J. Sugrue, and A.J. Hay (1992). Evidence that the amantadine-induced, M2-mediated
conversion of influenza A virus hemagglutinin to the low pH conformation occurs
in an acidic trans Golgi compartment. Virology 188(1): 14-24. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Amantadine treatment of cells infected with H7
strains of influenza A viruses causes an M2 protein-mediated conversion of
hemagglutinin (HA) from its native to its low pH conformation.
Immunofluorescence and electron microscopic observations showed that the
structural alteration and hence drug action occur shortly after HA exits from
the Golgi complex during its passage through the strans Golgi region. Using the
DAMP/anti-DNP pH probe it is evident that virus infection causes increased
acidity of the trans Golgi region and that vesicles containing low pH HA in
amantadine-treated virus-infected cells are particularly acidic. These results
indicate therefore that the alteration in HA is the direct consequence of
exposure to an adverse low pH and provide further support for the conclusion
that the M2 protein, the target of amantadine action, is involved in regulating
vesicular pH, a function important for the correct maturation of the HA
glycoprotein.
Descriptors: amantadine pharmacology, Golgi apparatus
metabolism, hemagglutinins viral chemistry, influenza A virus avian drug
effects, cell compartmentation, cultured cells, fluorescent antibody technique,
hemagglutinin glycoproteins, influenza virus, hemagglutinins viral drug
effects, hemagglutinins viral metabolism, hydrogen-ion concentration, avian ultrastructure,
microscopy, immunoelectron, monensin pharmacology, protein conformation drug
effects, temperature.
Ciampor, F., C.A. Thompson, S. Grambas, and A.J. Hay
(1992). Regulation of pH by the M2 protein of influenza A viruses. Virus
Research 22(3): 247-58. ISSN:
0168-1702.
NAL
Call Number: QR375.V6
Abstract: Inhibition of the function of the M2 protein
by amantadine can cause a conformational change in the haemagglutinin (HA) of
H7 influenza A viruses and the consequent expression of the low pH form of the
glycoprotein on the surface of virus-infected cells. Immunofluorescence studies
showed that this conversion occurs shortly after HA exists from the Golgi
complex apparently during its transport through the trans Golgi network and
using the pH probe, DAMP/anti-DNP, that it is the direct result of reduced
vesicular pH. The lowest pHs encountered were estimated using mutant HAs
differing in pH stability to be approximately 5.2 and 5.6 in virus-infected CEF
or MDCK cells, respectively, in the absence of functional M2. Depending on the
particular M2, this protein was responsible for increases in vesicular pH of up
to 0.8 units. The influence of mutations in both HA and M2 on the maturation of
native HA illustrates the important relationship between the structural and
functional properties of these two proteins. Using the fluorescent probe
SNARF-1 the M2 protein was also shown to be largely responsible for the 0.3-0.4
unit reduction in intracellular pH of virus-infected cells. The data thus provide
further evidence for the pH regulatory function of M2 and its importance for
the maturation of the HA glycoprotein.
Descriptors: influenza A virus avian physiology, viral
matrix proteins physiology, amantadine pharmacology, cell line, fluorescent antibody
technique, hemagglutination, viral, hydrogen-ion concentration.
Ciampor, F. and P. Turcan (1972). Electron
microscopy of tissue culture cells infected with myxoviruses. II.
Nucleo-cytoplasmic changes in fowl plague virus-infected cells. Acta
Virologica 16(3): 177-82. ISSN:
0001-723X.
NAL
Call Number: 448.3 AC85
Descriptors: cell nucleus microbiology, cultured cells
microbiology, cytoplasm microbiology, influenza A virus avian growth and
development, orthomyxoviridae growth and development, cell membrane
microbiology, cell nucleolus, cultured cells cytology, chick embryo,
cytopathogenic effect, viral, hamsters, inclusion bodies, viral, kidney
cytology, microscopy, electron, time factors, virus replication.
Clements, M.L., S.D. Sears, K. Christina, B.R.
Murphy, and M.H. Snyder (1989). Comparison of the virologic and immunologic
responses of volunteers to live avian-human influenza A H3N2 reassortant virus
vaccines derived from two different avian influenza virus donors. Journal
of Clinical Microbiology 27(1): 219-22.
ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: We compared the abilities of the six internal
RNA segments of two avian influenza viruses, A/Mallard/Alberta/88/76 (H3N8) and
A/Mallard/NY/6750/78 (H2N2), to confer attenuation on wild-type human influenza
A/Bethesda/1/85 (H3N2) virus in seronegative adult volunteers. Live avian-human
influenza A reassortant virus vaccines derived from either avian virus parent
were comparable in the following properties: safety, infectivity, immunogenicity,
and genetic stability. Since the avian influenza A/Mallard/Alberta/76 virus
offered no clear advantage as a donor virus, we will conduct our future
evaluations on live influenza A virus reassortants derived from the more
extensively characterized avian influenza A/Mallard/NY/78 virus.
Descriptors: antibodies, viral biosynthesis, influenza
prevention and control, influenza A virus avian immunology, human immunology,
influenza vaccine immunology, dose response relationship, immunologic,
electrophoresis, polyacrylamide gel, enzyme linked immunosorbent assay, genes
viral, hemagglutination inhibition tests, avian genetics, avian physiology,
human genetics, human physiology, influenza vaccine adverse effects, vaccines,
attenuated adverse effects, vaccines, attenuated immunology, vaccines,
synthetic adverse effects, vaccines, synthetic immunology, virus replication.
Clements, M.L., M.H. Snyder, A.J. Buckler White, E.L.
Tierney, W.T. London, and B.R. Murphy (1986). Evaluation of avian-human
reassortant influenza A/Washington/897/80 x A/Pintail/119/79 virus in monkeys
and adult volunteers. Journal of Clinical Microbiology 24(1):
47-51. ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: A reassortant influenza A virus was produced
by mating an avian influenza A/Pintail/Alberta/119/79 (H4N6) virus with
wild-type human influenza A/Washington/897/80 (H3N2) virus. The avian-human
influenza A reassortant virus contained the genes coding for the hemagglutinin
and neuraminidase surface antigens of the human influenza wild-type virus and
the six other RNA segments (internal genes) of the avian influenza A virus
donor. In the lower respiratory tract of squirrel monkeys, this avian-human
influenza reassortant virus, like its avian influenza A parent virus, was restricted
approximately 100-fold in replication compared with the wild-type human
influenza A virus. Despite this restriction of replication, infection of
monkeys with the avian-human influenza A reassortant virus induced resistance
to wild-type human influenza A virus challenge. In comparison with the
wild-type human influenza A virus, the avian-human influenza A reassortant was
also fully attenuated when 10(5.5) to 10(7.5) 50% tissue culture infective
doses were administered to susceptible adult volunteers. Attenuation was
indicated by a more than 300-fold reduction in virus shedding and lack of
reactogenicity. The reassortant virus did not spread to susceptible contacts
and could not be isolated from the blood or stools of infected adults. The 50%
human infectious dose was 10(6.2) 50% tissue culture infective dose, indicating
that this reassortant virus is only slightly less infectious for adults than a
similarly derived avian-human influenza A/Washington/80 X A/Mallard/78
reassortant virus. These findings suggest that the avian influenza A/Pintail/79
virus may be a satisfactory donor of attenuating genes for production of live,
attenuated avian-human influenza A reassortant virus vaccines.
Descriptors: influenza A virus human immunology,
immunology, influenza vaccine immunology, adolescent, adult, genes viral,
influenza immunology, influenza prevention and control, human genetics,
genetics, influenza vaccine adverse effects, saimiri, vaccines, attenuated
adverse effects, vaccines, attenuated immunology, virus replication.
Clements, M.L., E.K. Subbarao, L.F. Fries, R.A.
Karron, W.T. London, and B.R. Murphy (1992). Use of single-gene reassortant
viruses to study the role of avian influenza A virus genes in attenuation of
wild-type human influenza A virus for squirrel monkeys and adult human
volunteers. Journal of Clinical Microbiology 30(3): 655-62. ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: The transfer of six internal RNA segments
from the avian influenza A/Mallard/New York/6750/78 (H2N2) virus reproducibly
attenuates human influenza A viruses for squirrel monkeys and adult humans. To
identify the avian influenza A virus genes that specify the attenuation and
host range restriction of avian-human (ah) influenza A reassortant viruses (referred
to as ah reassortants), we isolated six single-gene reassortant viruses (SGRs),
each having a single internal RNA segment of the influenza A/Mallard/New
York/6750/78 virus and seven RNA segments from the human influenza A/Los
Angeles/2/87 (H3N2) wild-type virus. To assess the level of attenuation, we
compared each SGR with the A/Los Angeles/2/87 wild-type virus and a 6-2 gene ah
reassortant (having six internal RNA segments from the avian influenza A virus
parent and two genes encoding the hemagglutinin and neuraminidase glycoproteins
from the wild-type human influenza A virus) for the ability to replicate in
seronegative squirrel monkeys and adult human volunteers. In monkeys and
humans, replication of the 6-2 gene ah reassortant was highly restricted. In
humans, the NS, M, PB2, and PB1 SGRs each replicated significantly less
efficiently (P less than 0.05) than the wild-type human influenza A virus
parent, suggesting that each of these genes contributes to the attenuation
phenotype. In monkeys, only the NP, PB2, and possibly the M genes contributed
to the attenuation phenotype. These discordant observations, particularly with
regard to the NP SGR, indicate that not all genetic determinants of attenuation
of influenza A viruses for humans can be identified during studies of SGRs
conducted with monkeys. The PB2 and M SGRs that were attenuated in humans each
exhibited a new phenotype that was not observed for either parental virus.
Thus, it was not possible to determine whether avian influenza virus PB2 or M gene
itself or a specific constellation of avian and human influenza A virus
specified restriction of virus replication in humans.
Descriptors: influenza A virus avian genetics, human
genetics, adult, base sequence, genes viral, human pathogenicity, human
physiology, influenza vaccine isolation and purification, molecular sequence
data, RNA viral genetics, saimiri, transfection, vaccines, attenuated isolation
and purification, virulence genetics, virus replication genetics.
Cmarkova, J., D. Cmarko, E. Zavodska, A. Ellinger, M.
Pavelka, and F. Ciampor (1995). Ultrastructural lectinocytochemistry of fowl
plague virus-infected and uninfected MDCK cells. Acta Virologica
39(2): 85-93. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Using horseradish peroxidase (HRP)-conjugated
lectins for pre-embedding labelling we have shown differences in
ultrastructural localization of saccharides in cell compartments of fowl plague
(FP) virus-infected and uninfected MDCK cells. Lectinochemical staining of the cell
compartments in the case of FP virus-infected MDCK cells was less intensive as
compared with uninfected cells. Also certain differences in the staining of
subcompartments of cell organells were seen. Staining of uninfected cells with
Pisum sativum agglutinin (PSA)-HRP revealed an extensive visualization of Golgi
complex, mainly its cis-part, TGN vesicles and lysosomes. Staining of FP
virus-infected cells with the same lectin marked very lightly rough endoplasmic
reticulum and not at all the Golgi complex. Staining with Erythrina
cristagalli agglutinin (ECA)-HRP revealed a picture very similar to PSA-HRP
staining of uninfected and FP virus-infected cells. The differences in the
lectinochemical staining of cell organelles of FP virus-infected and uninfected
cells may be connected with the inhibition of cell protein synthesis during FP
virus morphogenesis.
Descriptors: influenza A virus avian chemistry, plant
lectins, antibodies, monoclonal immunology, cell line, dogs, hemagglutinin
glycoproteins, influenza virus, hemagglutinins viral metabolism, hemagglutinins
viral ultrastructure, immunoenzyme techniques, avian ultrastructure, lectins
metabolism.
Condobery, P.K. and R.D. Slemons (1992). Biological
properties of waterfowl-origin type A influenza viruses in chickens. Avian
Diseases 36(1): 17-23. ISSN:
0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: The replicative abilities and tissue tropism
properties of 13 non-pathogenic or low-pathogenic waterfowl-origin type A
influenza isolates recovered in 1986 were examined in chickens. Following
intravenous challenge, reisolation of challenge virus was attempted from swabs
of the luminal surfaces of the cloaca, jejunum, ileum, bursa, trachea, and air
sacs and from swabs of bone marrow and liver tissues. Virus-isolation attempts
were also accomplished on brain, thymus, spleen, pancreas, gonad, kidney,
blood, and lung tissues. The overall frequency of influenza virus recovery for
each experiment ranged from 3.1% to 49.3%. For all experiments combined, 58.3%
of the kidney tissues and 62.9% of the cloacal swab samples collected on days 1
to 10 postinoculation were positive for challenge virus recovery. Virus titers
up to 10(8.7) mean embryo infective dose per gram of kidney tissue were
demonstrated in clinically normal chickens. Distinct biological variations and
nephrotropism appear to exist among the corporate properties of virus
populations making up each of the 13 waterfowl-origin type A influenza
isolates.
Descriptors: chickens, fowl plague microbiology, influenza
A virus avian physiology, virus replication, antibodies, viral blood, chick
embryo, cloaca microbiology, avian immunology, avian isolation and
purification, kidney microbiology, serial passage, specific pathogen free
organisms.
Connor, R.J., Y. Kawaoka, R.G. Webster, and J.C.
Paulson (1994). Receptor specificity in human, avian, and equine H2 and H3
influenza virus isolates. Virology 205(1): 17-23. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: The receptor specificity of 56 H2 and H3
influenza virus isolates from various animal species has been determined to
test the relevance of receptor specificity to the ecology of influenza virus.
The results show that the receptor specificity of both H2 and H3 isolates
evaluated for sialic acid linkage specificity and inhibition of
hemagglutination by horse serum correlates with the species of origin, as
postulated earlier for H3 strains based on a limited survey of five human,
three avian, and one equine strain. Elucidation of the amino acid sequence of several
human H2 receptor variants and analysis of known sequences of H2 and H3
isolates revealed that receptor specificity varies in association with an amino
acid change at residues 228 in addition to the change at residue 226 previously
documented to affect receptor specificity of H3 but not H1 isolates. Residues
226 and 228 are leucine and serine in human isolates, which preferentially bind
sialic acid alpha 2,6-galactose beta 1,4-N-acetyl glucosamine (SA alpha
2,6Gal), and glutamine and glycine in avian and equine isolates, which exhibit
specificity for sialic acid alpha-2,3-galactose beta-1,3-N-acetyl galactosamine
(SA alpha 2,3Gal). The results demonstrate that the correlation of receptor
specificity and species of origin is maintained across both H2 and H3 influenza
virus serotypes and provide compelling evidence that influenza virus hosts
exert selective pressure to maintain the receptor specificity characteristics
of strains isolated from that species.
Descriptors: influenza A virus avian metabolism, human
metabolism, metabolism, receptors, virus metabolism, amino acid sequence, amino
acids genetics, carbohydrate sequence, chick embryo, hemagglutinin
glycoproteins, influenza virus, hemagglutinins viral genetics, molecular
sequence data, species specificity, viral envelope proteins genetics.
Content, J. (1976). Cell-free translation of
influenza virus mRNA. Journal of Virology 18(2): 604-18. ISSN: 0022-538X.
NAL
Call Number: QR360.J6
Abstract: Cytoplasmic poly (A)-rich RNA extracted from
fowl plague virus-infected cells was found to program efficiently the
translation of two major peptides in the wheat germ cell-free system. These
peptides have the same electrophoretic mobility, on polyacrylamide gels, as the
two major virion proteins M and NP. [35S] methionine tryptic peptide analysis
by one-dimensionalthin-layer ionophoresis and finger printing by
two-dimensional thin-layer ionophoresis and chromatography show a high degree
of similarity between the two in vitro products and the authentic viral proteins
M and NP. Although virion RNA is devoid of any poly (A) sequence, it is
confirmed here that the viral complementary cytoplasmic RNA contains poly (A)
stretches of varying lengths. Intact purified virion was found to promote the
synthesis of very low amounts of the same NP and M proteins in this cell-free system. Quantitative aspects
of data would indicate that this is due to minute amounts of complementary
viral RNA associated with the virion or with the virion RNA itself. In
conclusion, it is shown diectly by cell-free translation of authentic viral
products that the influenza virion is "negative stranded" (Baltimore,
1971), at least for its two major structural proteins.
Descriptors: influenza A virus avian metabolism, RNA,
messenger metabolism, RNA viral metabolism, translation, genetic, cell free
system, glycoproteins biosynthesis, avian analysis, peptide synthesis, plant
extracts, poly A analysis, RNA, messenger analysis, viral analysis, tissue
culture, triticum, viral proteins biosynthesis.
Content, J. (1969). Virus growth inhibition by
ethidium chloride and other dyes. Archiv Fur Die Gesamte Virusforschung
26(1): 74-85. ISSN: 0003-9012.
NAL
Call Number: 448.3 Ar23
Descriptors: dactinomycin pharmacology, dyes pharmacology,
virus replication drug effects, acridines pharmacology, carbon isotopes, chick
embryo, encephalitis viruses drug effects, encephalomyocarditis virus drug
effects, fibroblasts, herpesviridae drug effects, influenza A virus avian drug
effects, light, Newcastle disease virus drug effects, orotic acid metabolism,
polioviruses drug effects, tissue culture, uridine metabolism, vaccinia virus
drug effects.
Content, J., L.D. Wit, and M. Horisberger (1977). Cell-free
coupling of influenza virus RNA transcription and translation. Journal
of Virology 22(2): 247-55. ISSN:
0022-538X.
NAL
Call Number: QR360.J6
Abstract: A cell-free coupled system for the
transcription and translation of fowl plague virus RNA is described. The system
utilizes a new nuclease-preincubated rabbit reticulocyte lysate that has a high
sensitivity to exogenous mRNA and a very low level of nuclease activity.
Translation of the viral proteins in the coupled system is strictly dependent
upon the viral transcriptase activity. In the coupled system the optimal concentration
of magnesium is intermediate between the optimum for transcription and that for
translation. Translation of the viral proteins seems faithful. The products
represent the major viral peptides M and NP and two peptides with the same
electrophoretic mobility as HA and P2. Viron NA is not resolved in the kind of
polyacrylamide gels described. Proteins M and NP were immunoprecipitable with
monospecific antisera. It is concluded that the virion-associated RNA
polymerase transcribes the negative-stranded segments of the viral genome
coding for these major structural proteins into fully functional mRNA's.
Descriptors: influenza A virus avian metabolism, RNA viral
metabolism, transcription, genetic, translation, genetic, cell free system,
avian enzymology, magnesium metabolism, oligonucleotides pharmacology, peptide
synthesis, RNA replicase metabolism, messenger metabolism, viral biosynthesis,
rabbits, reticulocytes, viral proteins biosynthesis.
Conti, G. and P. Portincasa (2002). Chromomycin A3
inhibits influenza a virus multiplication in chick embryo fibroblast cells.
New Microbiologica Official Journal of the Italian Society for Medical,
Odontoiatric, and Clinical Microbiology SIMMOC 25(4): 385-98. ISSN: 1121-7138.
NAL
Call Number: QR1.M57
Abstract: The multiplication of Ulster 73 virus, an
avian strain of type A influenza virus, was blocked in chick embryo fibroblast
cells, CEF, by treatment with 0.5 microg/ml of chromomycin A3 whereas in
LLC-MK2 cells no inhibition of replication was observed. Virus-induced
polypeptide synthesis in chick embryo fibroblast cells was confined to the
synthesis of PB2, PB1 and PA subunits of the RNA dependent-RNA polymerase, the
nucleoprotein NP, the non-structural protein NS1, the haemagglutinin HA, the
non-structural protein NS2; only the membrane M1 polypeptide synthesis was
greatly inhibited. Viral unpolyadenylated cRNAs synthesis was studied at a late
time of the infection, 8 hours p.i.: chromomycin A3 was able to inhibit the
"novo" synthesis of complementary RNA poly(A)- and segment 7 of
virion RNA. The mode of action of the drug in chick embryo fibroblast cells is
discussed.
Descriptors: chromomycin A3 pharmacology, fibroblasts drug
effects, influenza A virus avian drug effects, nucleic acid synthesis
inhibitors pharmacology, virus replication drug effects, cell line, chick
embryo, electrophoresis, polyacrylamide gel, fibroblasts virology, avian
physiology, RNA viral biosynthesis, RNA viral genetics, virus cultivation.
Conti, G., P. Portincasa, and C. Chezzi (1995). Cerulenin
inhibits production of mature virion particles in chick embryo fibroblasts
infected by influenza A viruses. Research in Virology 146(2):
141-9. ISSN: 0923-2516.
NAL
Call Number: QR355.A44
Abstract: We investigated acylation of haemagglutinin
(HA) of type A influenza viruses during infection of permissive chick embryo
fibroblasts (CEF) treated with cerulenin. Fatty acid binding was monitored
using a maintenance medium containing 3H-palmitic acid. Our results suggest
that fatty acid acylation of viral haemagglutinin may be essential for
production of mature viral particles. Indeed, palmitoylation was found in
infected CEF cells, but was lacking during the infectious cycle when cells were
treated with a dose of 30 micrograms/ml of cerulenin. We discuss the
possibility that acylation of virus-induced HA is a posttranslational
modification regulating correct insertion of virus haemagglutinin into the
cellular membrane and, as a consequence, controlling the maturation of budding
influenza virus.
Descriptors: antiviral agents pharmacology, cerulenin
pharmacology, influenza A virus avian drug effects, virion drug effects,
acylation, cells,cultured, chick embryo, dose response relationship, drug,
fatty acids metabolism, fibroblasts cytology, hemagglutinin glycoproteins
influenza virus, hemagglutinins viral metabolism, avian metabolism, avian
physiology, virus replication drug effects.
Conti, G., P. Portincasa, C. Chezzi, and A. Sanna
(1988). Inhibition of late influenza virus genome expression by
diamidinophenylindole. Annales De L'Institut Pasteur. Virology
139(1): 69-78. ISSN: 0769-2617.
NAL
Call Number: QR355.A44
Abstract: The growth cycle of influenza virus strain
FPV, Ulster 73, was altered by treatment of LLC-MK2 cells with
diamidinophenylindole. Viral protein synthesis was restricted to the early
pattern of virus multiplication, and post-treatment experiments showed the
ability of the drug to block virus replication until the 4th hour p.i. Drug
addition (followed by removal) revealed the inhibition of synthesis of late
viral products, and especially of membrane protein. Kinetic studies on the
production of viral RNA indicated a decrease in the synthesis of late
virus-induced RNA species, suggesting that the target of DAPI is probably the
late transcription of the virus genome. The nonpermissive condition mediated by
the drug could represent a suitable model to study cellular intervention during
viral growth.
Descriptors: indoles pharmacology, influenza A virus avian
growth and development, virus replication drug effects, capsid genetics, gene
expression regulation drug effects, avian genetics, RNA viral biosynthesis, RNA
viral genetics, time factors, viral core proteins genetics, viral nonstructural
proteins.
Conti, G., P. Portincasa, A. Pesce, and C. Chezzi
(1985). Biological characterization of FPV, Ulster 73, replicative cycle.
Microbiologica 8(2): 151-64. ISSN: 0391-5352.
NAL
Call Number: QR1.M57
Abstract: The replication of an avian influenza A, Fowl
plague virus (FPV), Ulster 73 strain, was studied in chick embryo fibroblasts,
assumed to be the natural host, and in cells of different origin such as
LLC-MK2, Hep-2, Vero, KB and Mc Coy. In the natural host, FPV shows a characteristic
pattern of polypeptide synthesis suggesting a transcriptional and/or
translational mediated control mechanism, specific for this strain of influenza
A. FPV was able to give a productive infection in all the above mentioned cells
releasing mature viral particles. This behaviour is very interesting if one
compares FPV, Ulster strain to FPV, Rostock strain. These viruses, belonging to
the same antigenic subtype (H7 N1 group) recognize the same cellular
determinants but Rostock strain undergoes an abortive replication whereas
Ulster strain gives productive infection in all cellular lines tested. These
observations lead to postulate a viral genetic mechanism controlling host range
both at early and late steps in infection. This genetic mechanism controls the
interaction between viral and cell molecules affecting synthesis of virus
specific polypeptides.
Descriptors: influenza A virus avian physiology, virus
replication, chick embryo, dactinomycin pharmacology, avian genetics, RNA
viral analysis, viral proteins analysis, viral proteins biosynthesis, viral
structural proteins.
Conti, G., P. Valcavi, A. Natali, and G.C. Schito
(1980). Different patterns of replication in influenza virus-infected KB
cells. Archives of Virology 66(4): 309-20. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: When KB cells were infected either with the
fowl plague (FPV) Rostock strain (Hav1N1) or the WSN (H0N1) strain of influenza
A virus the yield of cell-associated haemagglutinin and neuraminidase
polypeptides was essentially comparable, but virus particles were not produced
in the FPV-KB system. WSN virus-infected KB cells synthesized normal amounts of
mature virus particles and had all the characteristics of a permissive
replication cycle. Biosynthesis and transport of RNP antigen from nucleus to
cytoplasm of infected cells were traced by immunofluorescent staining at 4 and
8 hours after the beginning of infection. While the fluorescent-stained
material was totally confined to the nuclei in FPV-infected KB cells, RNP antigen
migrated out of the nucleus during the replicative cycle of WSN virus in the
same host cell. Patterns of virus-specific protein synthesis were studied by
pulse-labelling with 35S-methionine. The most significant feature concerned the
amplification of synthesis of virus-induced matrix (M) protein which did not
occur in FPV-infected cells but occurred normally during WSN infection. The
different patterns of replication in the same host cell when infected by
different influenza A viruses is discussed.
Descriptors: influenza A virus avian growth and
development, human growth and development, cell line, cytopathogenic effect,
viral, hemagglutinins viral analysis, avian metabolism, human metabolism,
neuraminidase metabolism, ribonucleoproteins metabolism, viral proteins
biosynthesis, virus replication.
Cook, R.F., R.J. Avery, and N.J. Dimmock (1980). Complementation
with an avian influenza virus is required for synthesis of M protein of a human
strain in chicken erythocytes. Archives of Virology 65(3-4): 319-24. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The M protein of avian, but not human,
strains of influenza A viruses is synthesized in infected chicken erythrocytes.
In dual infections an avian strain complemented the human virus and both the
human and avian M proteins were expressed.
Descriptors: erythrocytes microbiology, influenza A virus
avian metabolism, human metabolism, viral proteins biosynthesis, chick embryo,
dactinomycin pharmacology, avian growth and development, human growth and
development.
Cook, R.F., R.J. Avery, and N.J. Dimmock (1979). Infection
of chicken erythrocytes with influenza and other viruses. Infection and
Immunity 25(1): 396-402. ISSN:
0019-9567.
NAL
Call Number: QR1.I57
Abstract: Chicken erythrocytes can be infected by the
fowl plague (Rostock) strain (FP/R) of influenza type A, Newcastle disease
virus (NDV), and Semliki Forest virus (SFV). Only NDV and SFV produced
infectious progeny, albeit at low levels. Infection by FP/R was monitored by de
novo synthesis of viral proteins, and the proteins synthesized could be
identified by comparison with infected chicken fibroblast cells. FP/R
synthesized far greater amounts of viral protein than did NDV or SFV.
Descriptors: erythrocytes microbiology, chick embryo,
hemagglutinins viral analysis, influenza A virus avian growth and development,
avian metabolism, leukocytes microbiology, neuraminidase metabolism, Newcastle
disease virus growth and development, Newcastle disease virus metabolism,
Semliki Forest virus growth and development, Semliki Forest virus metabolism,
viral proteins biosynthesis.
Cooper, L.A. and K. Subbarao (2000). A simple
restriction fragment length polymorphism-based strategy that can distinguish
the internal genes of human H1N1, H3N2, and H5N1 influenza A viruses. Journal
of Clinical Microbiology 38(7): 2579-83.
ISSN: 0095-1137.
NAL
Call Number: QR46.J6
Abstract: A simple molecular technique for rapid
genotyping was developed to monitor the internal gene composition of currently
circulating influenza A viruses. Sequence information from recent H1N1, H3N2,
and H5N1 human virus isolates was used to identify conserved regions within
each internal gene, and gene-specific PCR primers capable of amplifying all
three virus subtypes were designed. Subtyping was based on subtype-specific
restriction fragment length polymorphism (RFLP) patterns within the amplified
regions. The strategy was tested in a blinded fashion using 10 control viruses
of each subtype (total, 30) and was found to be very effective. Once
standardized, the genotyping method was used to identify the origin of the
internal genes of 51 influenza A viruses isolated from humans in Hong Kong
during and immediately following the 1997-1998 H5N1 outbreak. No avian-human or
H1-H3 reassortants were detected. Less than 2% (6 of 486) of the RFLP analyses
were inconclusive; all were due to point mutations within a restriction site.
The technique was also used to characterize the internal genes of two avian
H9N2 viruses isolated from children in Hong Kong during 1999.
Descriptors: genes viral, influenza virology, influenza A
virus human classification, human genetics, polymorphism, restriction fragment
length, disease outbreaks, Hong Kong, avian classification, avian genetics,
avian isolation and purification, human isolation and purification, reverse
transcriptase polymerase chain reaction.
Corfield, A.P., H. Higa, J.C. Paulson, and R. Schauer
(1983). The specificity of viral and bacterial sialidases for alpha(2-3)-
and alpha(2-6)-linked sialic acids in glycoproteins. Biochimica Et
Biophysica Acta 744(2): 121-6. ISSN:
0006-3002.
NAL
Call Number: 381 B522
Abstract: The anomeric specificity of six sialidases (Vibrio
cholerae, Arthrobacter ureafaciens, Clostridium perfringens, Newcastle
disease virus, fowl plague virus and influenza A2 virus sialidases) was
assessed with sialylated antifreeze glycoprotein, ovine submandibular gland
glycoprotein and alpha 1-acid glycoprotein, resialylated specifically in
alpha(2-3) or alpha(2-6) linkage with N-acetylneuraminic acid or
N-glycolylneuraminic acid using highly purified sialyltransferases. The rate of
release of sialic acid from these substrates was found to correlate well with
the specificity observed earlier with the same sialidases using small oligosaccharide
substrates, i.e., alpha(2-3) glycosidic linkages are hydrolyzed faster than
alpha(2-6) linkages, with the exception of the enzyme from A. ureafaciens.
Sialidase activity was higher with N-acetylneuraminic acid when compared with
N-glycolylneuraminic acid. The studies also showed that the core
oligosaccharide and protein structure in glycoproteins may influence the rate
of release for different glycosidic linkages.
Descriptors: glycoproteins metabolism, neuraminidase
metabolism, sialic acids metabolism, arthrobacter enzymology, Clostridium
perfringens enzymology, influenza A virus avian enzymology, enzymology,
Newcastle disease virus enzymology, structure activity relationship, substrate
specificity, vibrio cholerae enzymology.
Corfield, A.P., M. Wember, R. Schauer, and R. Rott
(1982). The specificity of viral sialidases. The use of oligosaccharide
substrates to probe enzymic characteristics and strain-specific differences.
European Journal of Biochemistry FEBS 124(3): 521-5. ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: 1. The action of sialidases from Newcastle
disease virus (NDV), influenza A2 virus (IA2V) and fowl plague virus (FPV) on
sialyloligosaccharide substrates containing alpha 2-3, alpha 2-6 or alpha 2-8
linkages was studied. 2. In all cases 2-3-linked sialic acids were
preferentially released. Compared with II6Neu5AcLac, all 2-6-linked substrates,
including sialyl-N-acetyllactosamine and its asparaginyl derivative, a urinary
hexasaccharide and Neu5Ac(2-6)GalNAc were cleaved at improved rates by NDV and
less by FPV sialidases. In the case of IA2V sialidase the asparaginyl
oligosaccharide was very poorly cleaved, illustrating a variation in viral
strain specificity. 3. A decrease in relative rates was observed in the order NDV
greater than IA2V greater than FPV for substrates with 2-3 linkages relative to
II6Neu5AcLac. The greatest relative rate was 470-fold higher. The 2-3-linked
sialyl-N-acetyllactosaminylasparagine and IV3Neu5AcLcOse4 were poor substrates
for the IA2V sialidase, but the rates were greater than with the 2-6 linked
substrates. 4. The ganglioside substrate II3Neu5AcLacCer showed lower activity
than its oligosaccharide analogue, but neither II3Neu5AcGgOse4Cer nor its
oligosaccharide were substrates. 5. The Km values for 2-6-linked substrates
were generally of the order 10 mM while those for the 2-3-linked substrates
were approximately 1 mM. The V values were consistently higher for the
2-3-linked substrates. IV3Neu5AcLcOse4 showed high Km and very high V values, while
the 2-8-linked disialyllactose showed this trend only with NDV enzyme, the IA2V
and FPV sialidases exhibiting high Km and low V values. 6. The results are
discussed in the light of the current knowledge of viral sialidase specificity
and relative to the binding of virus particles to cell surfaces.
Descriptors: neuraminidase metabolism, oligosaccharides
metabolism, viruses enzymology, colorimetry, glycoproteins metabolism,
influenza A virus avian enzymology, enzymology, kinetics, Newcastle disease virus
enzymology, species specificity, substrate specificity.
Cox, N.J. and R.D. Barry (1976). Hybridization
studies of the relationship between influenza virus RNA and cellular DNA. Virology
69(1): 304-13. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: DNA analysis, influenza A virus avian
analysis, nucleic acid hybridization, RNA, ribosomal analysis, viral analysis,
bromelains pharmacology, genes, avian drug effects, avian isolation and
purification, kinetics, temperature, transcription, genetic.
Crawford, J.M., M. Garcia, H. Stone, D. Swayne, R.
Slemons, and M.L. Perdue (1998). Molecular characterization of the
hemagglutinin gene and oral immunization with a waterfowl-origin avian
influenza virus. Avian Diseases 42(3): 486-496. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: Vaccination against highly pathogenic (HP)
subtypes of avian influenza (AI) virus in poultry has been prohibited in the
United States. Recently, policy has been changed to potentially allow use of
inactivated vaccines in emergency programs to control HP H5 and H7 AI.
Vaccination with inactivated virus against non-highly pathogenic AI viruses has
been allowed in the U.S. turkey industry since 1979 (1) but requires expensive
handling of individual birds for parenteral inoculation. Oral immunization
would provide a less expensive method to protect commercial poultry from AI.
Prime candidates for oral vaccines are waterfowl-origin (WFO) isolates, which
have a tropism for the alimentary tract. One WFO isolate, A/mallard/Ohio/556/1987
(H5N9) (MOh87), was characterized by determining the complete nucleotide
sequence of its hemagglutinin (HA) gene. The HA protein of this isolate
possessed a deduced amino acid sequence nearly identical to the consensus amino
acid sequence for all published H5 genes, indicating that it has potential as a
broadly effective vaccine. Experimental results demonstrated measurable serum
antibody responses to orally delivered live and inactivated preparations of
MOh87. Oral vaccination also protected chickens from diverse, lethal H5 AI
virus challenge strains and blocked cloacal shedding of challenge virus.
Descriptors: avian influenza virus, chickens,
hemagglutinins, immunization, oral administration, genes, oral vaccination,
virulence, live vaccines, inactivated vaccines, experimental infections, strain
differences, nucleotide sequences, amino acid sequences, immune response,
molecular sequence data, GENBANK u67783.
Crescenzo Chaigne, B., S. van der Werf, and N.
Naffakh (2002). Differential effect of nucleotide substitutions in the 3'
arm of the influenza A virus vRNA promoter on transcription/replication by
avian and human polymerase complexes is related to the nature of PB2 amino acid
627. Virology 303(2):
240-52. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Using a genetic system that allows the in
vivo reconstitution of active ribonucleoproteins, the ability to ensure
transcription/replication of a viral-like reporter RNA harboring the G(3)
--> A(3), U(5) --> C(5), and C(8) --> U(8) mutations (triple 3-5-8
mutations) in the 3' arm of the promoter was examined with core proteins from
human or avian strains of influenza A viruses. The efficiency of
transcription/replication of the viral-like RNA with the triple 3-5-8 mutations
in COS-1 cells was found to be slightly decreased as compared to the wild-type
RNA when the polymerase was derived from a human virus. In contrast, it was
found to be considerably increased when the polymerase was derived from an
avian virus, in agreement with published observations using the avian
A/FPV/Bratislava virus (G. Neumann and G. Hobom, 1995, J. Gen. Virol. 76,
1709-1717). This increase could be attributed to the compensation of the defect
in transcription/replication activity in the COS-1 mammalian cell line due to
the presence of a glutamic acid at PB2 residue 627, characteristic of avian
strains of influenza viruses. Our results thus suggest that PB2 and/or cellular
proteins interacting with PB2 could be involved in RNA conformational changes
during the process of transcription/replication.
Descriptors: DNA directed RNA polymerases physiology,
influenza A virus avian enzymology, human enzymology, promoter regions
genetics, viral chemistry, transcription, genetic, viral proteins chemistry,
virus replication, amino acid sequence, base sequence, cos cells, molecular
sequence data, mutation, nucleic acid conformation, viral biosynthesis.
Crumpton, W.M., N.J. Dimmock, P.D. Minor, and R.J.
Avery (1978). The RNAs of defective-interfering influenza virus. Virology
90(2): 370-3. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: defective viruses analysis, influenza A virus
avian, RNA viral analysis, defective viruses growth and development, defective
viruses metabolism, viral proteins biosynthesis.
Dammgen, J.W. and C. Scholtissek (1975). Cellular
RNA and influenza-virion RNA are synthesized from different
pyrimidine-nucleoside-triphosphate pools in chick-embryo cells. European
Journal of Biochemistry FEBS 59(1): 51-4.
ISSN: 0014-2956.
NAL
Call Number: QP501.E8
Abstract: Chick embryo cells infected with an influenza
A (fowl plague) virus have been labelled with (3H)-uridine for different
lengths of time. Virion RNA and cellular RNA have been separated by specific
hybridization with a surplus of unlabelled viral complementary RNA and RNase
digestion. The ratio of the specific radioacticity in the UMP and CMP moieties
of both types of RNA has been determined. Since the rate of approach to
equilibrium of CMP to UMP labelling of both types of RNA is completely
different it is concluded that cellular and virion RNA are synthesized using
different pyrimidine nucleoside triphosphate pools.
Descriptors: influenza A virus avian metabolism,
pyrimidine nucleotides metabolism, RNA biosynthesis, RNA viral biosynthesis,
cells cultured, chick embryo, nucleic acid hybridization, transcription,
genetic, uridine metabolism.
Daniels, R.S., J.J. Skehel, and D.C. Wiley (1985). Amino
acid sequences of haemagglutinins of influenza viruses of the H3 subtype
isolated from horses. Journal of General Virology 66(Pt. 3):
457-64. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The amino acid sequence of the haemagglutinin
of A/equine/Miami/63 (H3N8), the prototype influenza virus of the H3 subtype
from horses, is deduced from the nucleotide sequence of virus RNA and compared
with the sequences of haemagglutinins of viruses of this subtype isolated from
humans [X-31 (H3N2)] and from birds [A/duck/Ukraine/63 (H3N8)] and with the
sequence of the haemagglutinin of A/equine/Fontainebleau/79 (H3N8) a virus
isolated from a recent outbreak of equine influenza. The amino acid sequence
differences detected are discussed with reference to the structure of the
molecules, their antigenicity and antigenic drift in influenza viruses viruses
isolated from horses.
Descriptors: hemagglutinins viral, influenza A virus
genetics, amino acid sequence, avian genetics, immunology, RNA viral genetics,
species specificity, horses.
Darveau, A., N.G. Seidah, M. Chretien, and J. Lecomte
(1982). Peptide mapping of 125I-labelled membrane protein of influenza
viruses by reverse-phase high-performance liquid chromatography. Journal
of Virological Methods 4(2): 77-85.
ISSN: 0166-0934.
NAL
Call Number: QR355.J6
Abstract: The resolution potential of reverse-phase
high-performance liquid chromatography (HPLC) for peptide analysis of
hydrophobic viral membranes has been investigated, using as model the membrane
(M) protein of influenza virus. Proteolytic digests of 125I-labelled M protein
and CNBr fragments, extracted from radioiodinated whole virus, have been
separated on a uBondapak C18 column with an isopropanol or acetonitrile solvent
system. Peptide mapping of trypsin digests of M protein from A/PR/8/34 (H1N1)
and A/chicken/Germany/N/49 (H10N7) viruses was identical, whereas Staphylococcus
aureus V8 protease digests showed minor differences in at least two
peptides. The results also show that HPLC is a powerful tool for the separation
of proteolytic digests of viral proteins, since the peptide maps are highly
reproducible and recovery was greater than 85%.
Descriptors: chromatography, high pressure liquid methods,
influenza A virus avian analysis, membrane proteins analysis, peptides
analysis, viral proteins analysis, electrophoresis, polyacrylamide gel, iodine
radioisotopes.
Datema, R., P.A. Romero, R. Rott, and R.T. Schwarz
(1984). On the role of oligosaccharide trimming in the maturation of Sindbis
and influenza virus. Archives of Virology 81(1-2): 25-39. ISSN: 0304-8608.
NAL
Call Number: 448.3 Ar23
Abstract: The alpha-glucosidase inhibitor
bromoconduritol inhibits the formation of the N-linked, complex-type
oligosaccharides of the glycoproteins from influenza viruses (fowl plague
virus, influenza virus PR-8) and from sindbis virus. Viral glycoproteins
produced in bromoconduritol-treated chicken-embryo and baby-hamster kidney
cells are fully glycosylated, but accumulate N-linked, high-mannose
oligosaccharides of the composition Glc1Manx (GlcNAc)2 (x = 7, 8, and 9). Other
alpha-glucosidase inhibitors (nojirimycin, deoxynojirimycin, acarbose) were not
specific inhibitors of oligosaccharide processing under the conditions used in
the present investigation. In bromoconduritol-treated, sindbis virus-infected
chicken-embryo and baby-hamster kidney cells, the sindbis glycoproteins are
metabolically stable. Specific proteolytic cleavage of the polyprotein
precursors to form E2 and E1 occurs in bromoconduritol-treated chicken-embryo
cells, but cleavage of PE2 to E2 is prevented in the infected baby-hamster
kidney cells. Yet, release of infectious sindbis virus particles is inhibited
in both cell types indicating that the formation of complex oligosaccharides is
required for a late step in virus formation. The release of virus particles
from influenza virus PR-8-infected bromoconduritol-treated chicken-embryo cells
is not inhibited, and virus with only high-mannose oligosaccharides is formed.
In contrast, when chicken-embryo cells were infected with the influenza virus
fowl plague virus, release of infectious particles was inhibited. The fowl
plague virus hemagglutinin is cleaved in chicken-embryo cells, in contrast to
the hemagglutinin of the PR-8 virus. However, the cleavage products HA1 and HA2
do not reach the cell surface. In addition, or as a consequence, HA1 and HA2
are proteolytically broken down, whereas uncleaved hemagglutinin of PR-8
appeared metabolically stable. These results may explain the decrease in
formation of fowl plague virus particles and the lack of effect on PR-8 virus
in bromoconduritol-treated cells. This work thus shows different biological
roles for oligosaccharide processing.
Descriptors: glycoproteins biosynthesis, influenza A virus
avian growth and development, oligosaccharides metabolism, sindbis virus growth
and development, viral proteins biosynthesis, cell line, chick embryo,
glycoproteins isolation and purification, glycoside hydrolases antagonists and
inhibitors, hamsters, avian drug effects, inositol analogs and derivatives,
inositol pharmacology, kidney, oligosaccharides isolation and purification,
sindbis virus drug effects, viral proteins isolation and purification.
Davenport, F.M., A.V. Hennessy, and E. Minuse (1968).
The age distribution in humans of hemagglutinating-inhibiting antibodies
reacting with avian strains of influenza A virus. Journal of Immunology
100(3): 581-5. ISSN: 0022-1767.
NAL
Call Number: 448.8 J8232
Descriptors: antibodies analysis, influenza immunology,
influenza A virus avian immunology, adolescent, adult, aged, aging, child,
child preschool, hemagglutination inhibition tests, infant, middle aged,
statistics.
Davey, J., S.M. Hurtley, and G. Warren (1985). Reconstitution
of an endocytic fusion event in a cell-free system. Cell 43(3 Pt.
2): 643-52. ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Abstract: Using a cell-free system we have obtained
fusion of vesicles from the endocytic pathway. The fusion is rapid, efficient,
and requires ATP. Only vesicles derived from certain positions along the
endocytic pathway are capable of fusing. Lysosomes and vesicles derived from
the plasma membrane do not fuse.
Descriptors: endocytosis, membrane fusion, adenosine
triphosphate physiology, cell line, cell membrane physiology, cell free system,
hamsters, influenza A virus avian, kidney, lysosomes physiology, mesocricetus,
Semliki Forest virus, sialic acids analysis.
Davies, P. and R.D. Barry (1966). Nucleic acid of
influenza virus. Nature 211(47): 384-7. ISSN: 0028-0836.
NAL
Call Number: 472 N21
Descriptors: orthomyxoviridae analysis, RNA viral
analysis, aphthovirus analysis, centrifugation, density gradient, encephalitis
viruses analysis, influenza A virus avian analysis, molecular weight, Newcastle
disease virus analysis, phosphorus isotopes, rauscher virus analysis, sarcoma
viruses, avian analysis, spectrum analysis.
Deibel, R., D.E. Emord, W. Dukelow, V.S. Hinshaw, and
J.M. Wood (1985). Influenza viruses and paramyxoviruses in ducks in the
Atlantic flyway, 1977-1983, including an H5N2 isolate related to the virulent
chicken virus. Avian Diseases 29(4): 970-85. ISSN: 0005-2086.
NAL
Call Number: 41.8 Av5
Abstract: From 1977 to 1983, waterfowl migrating along
the Atlantic flyway were annually monitored for orthomyxoviruses and
paramyxoviruses in an area in central New York State. A total of 168 influenza
isolates were obtained from 1,430 waterfowl. Twenty-four combinations of
hemagglutinin and neuraminidase subtypes were detected, with as many as 12
found in a single year. One combination, an H5N2 isolate in 1982, was closely
related to the virulent chicken virus that appeared in Pennsylvania in 1983.
The prevalence of influenza varied greatly among the common waterfowl species:
mallards 42%, black ducks 30%, blue-winged teal 11%, wood ducks 2%, and Canada
geese 0%. A total of 89 paramyxoviruses were also from these waterfowl. In
contrast to findings with influenza virus, the prevalence of paramyxoviruses
did not differ significantly among the duck species. Serotype 1 (Newcastle
disease virus) was predominant; three other serotypes were also identified.
These findings indicated that ducks in the Atlantic flyway continually harbor
influenza viruses and paramyxoviruses. The viruses may be a source of infection
for other species.
Descriptors: ducks microbiology, influenza A virus avian
isolation and purification, orthomyxoviridae isolation and purification,
paramyxoviridae isolation and purification, antigens, viral analysis,
demography, New York, species specificity.
Dem'ianenko, I.V., Z.I. Rovnova, E.I. Isaeva, and
Z.K. Chuvakova (1989 ). Antigennaia struktura gemaggliutininov virusov
grippa H1N1 (Hsw1N1), vydelennykh ot liudei i utok. [Antigenic structure of
hemagglutinins of influenza H1N1 (Hsw1N1) virus isolated from humans and ducks].
Voprosy Virusologii 34(6): 661-5.
ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: The method of specific adsorption followed by
the use of antisera in HI test and competitive enzyme immunoassay was used to
study the antigenic composition of hemagglutinins (HA) Hsw1 in influenza
viruses isolated in 1982 from humans in Bulgaria and in 1976 in Canada from
ducks as well as their antigenic relationships with HA of Hsw1 variant isolated
from swine and man. Hemagglutinins of Hsw1 strains isolated from man in
Bulgaria and Alma-Ata were found to be similar to HA of A/New Jersey/8/76 virus
in two determinants and with hemagglutinin of the classic virus of swine in
three determinants. The HA of A/duck/Alberta/35/76 virus was similar in three
determinants to HA of A/New Jersey/8/76 virus and in two determinants with
other Hsw1 variants. The similarities and differences in antigenic determinants
of HA in Hsw1 viruses isolated from man and animals attest to their common
origin and different modes of variability.
Descriptors: epitopes analysis, hemagglutinins viral
immunology, influenza A virus avian immunology, human immunology, ducks, enzyme
linked immunosorbent assay, immunosorbent techniques.
Dem'ianenko, I.V., A.A. Shilov, Z.K. Chuvakova, O.V.
Chaika, and E.I. Isaeva (1988). Sravnitel'naia kharakteristika
gemaggliutinov virusov grippa A s antigennoi strukturoi Hsw1N1, vydelennykh ot
cheloveka i zhivotnykh. [Comparative characteristics of hemagglutinins of
influenza A viruses with antigenic structure Hsw1N1 isolated from man and
animals]. Voprosy Virusologii 33(2): 157-62. ISSN: 0507-4088.
NAL
Call Number: 448.8 P942
Abstract: Competitive radioimmunoassay was used to
study the antigenic composition of hemagglutinin of Hsw1N1 viruses isolated
from man in comparison with hemagglutinin Hsw1 of influenza virus of swine and
ducks. The data of oligonucleotide analysis of the 4th RNA segment coding for
hemagglutinin in these viruses are presented. It has been shown that in
Alma-Ata, 1984-1985, influenza viruses Hsw1N1 were isolated with the antigenic
structure of hemagglutinin and with the hemagglutinin gene identical with those
of the classical influenza virus of swine A/Swine/Iowa/15/30 but differing from
virus A/New Jersey/8/76.
Descriptors: antigens, viral analysis, hemagglutinins
viral analysis, influenza A virus avian immunology, human immunology,
influenza A virus porcine immunology, immunology, adsorption, antigens, viral
genetics, binding, competitive, ducks, genes viral, hemagglutinins viral
genetics, avian genetics, avian isolation and purification, human genetics,
human isolation and purification, porcine genetics, porcine isolation and
purification, Kazakhstan, oligonucleotides analysis, oligonucleotides genetics
, RNA viral analysis, viral genetics,
radioimmunoassay methods, swine.
Desheva, J.A., L.G. Rudenko, G.I. Alexandrova, X. Lu,
A.R. Rekstin, J.M. Katz, N.J. Cox, and A.I. Klimov (2004). Reassortment
between avian apathogenic and human attenuated cold-adapted viruses as an
approach for preparing influenza pandemic vaccines. International
Congress Series 1263: 724-727.
Abstract: To prepare candidate influenza pandemic vaccines,
we are developing an approach based on reassortment of antigenically
appropriate nonpathogenic avian viruses of different subtypes (H5, H9, H7) with
the cold-adapted master strain (MS) A/Leningrad/134/17/57 (Len/17) that is
currently used in Russia for preparing licensed live attenuated vaccines for
adults and children. In the present study, reassortants between
A/Duck/Potsdam/1402-6/86(H5N2) (H5N2-wt) and Len/17 were obtained. One of the
clones, A/17/Duck/Potsdam/86-92(H5N2) (Len17/H5), was chosen for further
detailed genetic and antigenic analysis. Len17/H5 inherited the HA gene from
the H5N2-wt and all other genes from Len/17 (7:1 genome composition). The HA
gene sequence of Len17/H5 was identical to that of the parent H5N2-wt virus.
The antigenic profile of the reassortant virus was similar to that of the
H5N2-wt parent strain in the hemagglutination-inhibition (HI) test with a panel
of antisera to different avian and human H5 viruses. The reassortant
demonstrated high growth ability (9.3+0.3 lg EID50/ml) in embryonated hens'
eggs (CE) at optimal (34 [deg]C) temperature, comparable with that of the
parent Len/17 MS. Also, Len17/H5 demonstrated cold-adapted (ca) and
temperature-sensitive (ts) phenotypes similar to those of Len/17 and was
attenuated for mice.
Descriptors: avian influenza, live attenuated reassortant
vaccine.
Deshpande, K.L., V.A. Fried, M. Ando, and R.G.
Webster (1987). Glycosylation affects cleavage of an H5N2 influenza virus
hemagglutinin and regulates virulence. Proceedings of the National
Academy of Sciences of the United States of America 84(1): 36-40. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Based on nucleotide sequence analysis of the
hemagglutinin (HA) gene from the virulent and avirulent A/chicken/Pennsylvania/83
influenza viruses, it was previously postulated that acquisition of virulence
was associated with a point mutation that resulted in loss of a glycosylation
site. Since there are two potential glycosylation sites in this region of the
HA molecule and since all Asn-Xaa-Thr/Ser sequences in the HAs of different
strains are not necessarily glycosylated, the question remained open as to
whether either one of these sites was glycosylated. We now provide direct
evidence that a site-specific glycosylation affects cleavage of the influenza
virus HA and thus virulence. We have identified the glycosylation sites on the
HA1 subunit from the virulent and avirulent strains by direct structural
analysis of the isolated proteins. Our results show that the only difference in
glycosylation between the HA1s of the virulent and avirulent strains is the
lack of an asparagine-linked carbohydrate on the virulent HA1 polypeptide at
residue 11. Further, we show that the HA1s of both the avirulent and virulent
viruses are not glycosylated at one potential site, while all other sites
contain carbohydrate. Amino acid sequence analysis of the HA1 of an avirulent
revertant of the virulent strain confirmed these findings.
Descriptors: genes, structural, genes viral, glycoproteins
genetics, hemagglutinins viral genetics, influenza A virus avian pathogenicity,
amino acid sequence, chick embryo, chromatography, high pressure liquid,
glycopeptides analysis, hemagglutinins viral isolation and purification, avian
genetics, oligosaccharides analysis, peptide fragments analysis, trypsin,
virulence.
Deshpande, K.L., C.W. Naeve, and R.G. Webster (1985).
The neuraminidases of the virulent and avirulent A/Chicken/Pennsylvania/83
(H5N2) influenza A viruses: sequence and antigenic analyses. Virology
147(1): 49-60. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: To define the sequence changes that occurred
in an avian influenza virus neuraminidase (NA) during the evolution of
virulence, we have studied the NA of the virulent and avirulent A/Chick/Penn/83
(H5N2) influenza viruses. A comparison of the deduced amino acid sequence from
these viruses shows that the virulent strain, which evolved from the avirulent
by the accumulation of point mutations (Bean et al., 1985), acquired four amino
acid changes in the NA: one in the transmembrane segment, one in the stalk, and
two in the head. A comparison of the deduced amino acid sequences with those of
the human N2 NAs indicates a 20-amino acid deletion in the stalk of the
Chick/Penn/83 NA. Antigenic analysis of the NAs from the avirulent and virulent
Chick/Penn/83 virus shows they are antigenically very closely related, but can
be distinguished with two monoclonal antibodies at a site which probably
involves at least one of the amino acid changes in the NA head. Antigenic
analysis also shows the Chick/Penn/83 NAs are closely related to the NAs of
other N2 avian influenza viruses isolated between 1965 and 1984, supporting
previous studies which indicate a relative antigenic stability of the NA among
avian N2 influenza viruses. The Chick/Penn/83 NAs are the first N2 NA genes of
an avian virus to be sequenced. These NAs are antigenically closely related to
the 1957 human N2 NAs, and show a high degree of amino acid sequence homology
with the prototype 1957 human N2 NA. These data give further support to the
view that the 1957 human H2N2 viruses were at least partially derived from an
avian source.
Descriptors: influenza A virus avian enzymology,
neuraminidase isolation and purification, amino acid sequence, antibodies
monoclonal diagnostic use, base sequence, chick embryo, chickens, epitopes
analysis, genes structural, genes viral, avian genetics, avian pathogenicity,
models molecular, neuraminidase immunology, protein conformation, species
specificity, virulence.
Desselberger, U., K. Nakajima, P. Alfino, F.S.
Pedersen, W.A. Haseltine, C. Hannoun, and P. Palese (1978). Biochemical
evidence that "new" influenza virus strains in nature may arise by
recombination (reassortment). Proceedings of the National Academy of
Sciences of the United States of America 75(7): 3341-5. ISSN: 0027-8424.
NAL
Call Number: 500 N21P
Abstract: Oligonucleotide analysis of two avian
influenza A viruses (Hav6N2 and Hav6Nav4) isolated in nature showed identical
or almost identical patterns for the corresponding M and HA genes; 24 of 25 and
13 of 13 large oligonucleotides were indistinguishable by two-dimensional gel
analysis. On the other hand, remarkable differences in the oligonucleotide
patterns of the remaining genes were observed. Only 2 of 11 oligonucleotide
spots of the NS gene, 10 of 27 spots of the NA/NP genes, and 22 of 49 spots of
the P genes were indistinguishable between the two strains. On the basis of
this observation that at least two genes of these viruses are virtually
identical whereas others show easily detectable differences, we conclude that
the two avian strains are related to each other by a recombinational event. In
addition, it was found that animals in nature can be doubly infected with
influenza viruses. Both lines of evidence strongly suggest that recombination
is at least one mechanism by which "new" influenza virus strains
emerge in nature.
Descriptors: genes viral, influenza A virus avian
genetics, recombination, genetic, hemagglutinins viral analysis, avian
immunology, oligoribonucleotides analysis, RNA viral analysis.
Desselberger, U. and P. Palese (1978). Molecular
weights of RNA segments of influenza A and B viruses. Virology
88(2): 394-9. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Descriptors: influenza A virus analysis, orthomyxoviridae
analysis, RNA viral analysis, genes viral, hemagglutinins viral genetics, avian
analysis, human analysis, genetics, molecular weight, neuraminidase genetics,
nucleic acid denaturation, oligonucleotides analysis, orthomyxoviridae
genetics.
Diringer, H., W.R. Willems, and R. Rott (1978). Metabolism
of myoinositol in avian and mammalian cells infected with naked and enveloped
DNA and RNA viruses. Journal of General Virology 40(2): 471-4. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The uptake of 3H-inositol into the pool of
free inositol and its incorporation into the lipid phosphatidylinositol have
been studied in various avian and mammalian cells infected by different
viruses. In all the virus-cell systems investigated, virus infection results in
a drastically reduced amount of free 3H-inositol about 3 to 5 h post-infection,
demonstrable in the infected cells as compared to the mock-infected controls.
In contrast, the incorporation of 3H-inositol into lipid can be enhanced,
reduced, or not influenced at all, depending on the virus-cell system under
observation.
Descriptors: DNA viruses growth and development, inositol
metabolism, RNA viruses growth and development, adenoviruses, human growth and
development, birds, cell line, herpesvirus 1, suid growth and development,
influenza A virus avian growth and development, mammals, Newcastle disease
virus growth and development, phosphatidylinositols biosynthesis, polioviruses
growth and development, tissue culture.
Donatelli, I., L. Campitelli, M.R. Castrucci, A.
Ruggieri, L. Sidoli, and J.S. Oxford (1991). Detection of two antigenic
subpopulations of A(H1N1) influenza viruses from pigs: antigenic drift or
interspecies transmission? Journal of Medical Virology 34(4):
248-57. ISSN: 0146-6615.
Abstract: Serological analysis of a group of 63
influenza H1N1 viruses isolated from pigs in Italy in the period 1976-1988
revealed the presence of two distinct antigenic subpopulations: some viruses
possessed a haemagglutinin indistinguishable from that of viruses typically
associated with pigs, i.e., A/New Jersey/8/76 (H1N1), whereas others showed a
close antigenic relatedness with the haemagglutinin of avian-like H1 viruses.
These findings represent further evidence that influenza A viruses from avian
species may be transmitted to mammals. The surface and internal proteins of
some of these viruses were also analyzed biochemically to evaluate the
molecular relatedness among viruses circulating in non-human hosts.
Descriptors: hemagglutinins viral immunology, influenza A
virus avian immunology, porcine immunology, orthomyxoviridae infections
veterinary, swine microbiology, swine diseases microbiology, antibodies,
monoclonal immunology, antigenic variation, electrophoresis, polyacrylamide
gel, avian isolation and purification, porcine isolation and purification,
Italy, orthomyxoviridae infections microbiology, orthomyxoviridae infections
transmission, peptide mapping, species specificity.
Donis, R.O., W.J. Bean, Y. Kawaoka, and R.G. Webster
(1989). Distinct lineages of influenza virus H4 hemagglutinin genes in
different regions of the world. Virology 169(2): 408-17. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: To understand the determinants of influenza
virus evolution, phylogenetic relationships were determined for nine
hemagglutinin (HA) genes of the H4 subtype. These genes belong to a set of
viruses isolated from several avian and mammalian species from various
geographic locations around the world between 1956 and 1985. We found that the
HA gene of the H4 subtype is 1738 nucleotides in length and is predicted to
encode a polypeptide of 564 amino acids. The connecting peptide, which is
removed from the precursor polypeptide by peptidases to yield the mature HA1
and HA2 polypeptides, contains only one basic amino acid. This type of
connecting peptide is a feature of all avian avirulent HAs. On the basis of
pairwise nucleotide sequence homology comparisons the genes can be segregated
into two groups: influenza virus genes isolated in North America and those
isolated from other parts of the world. A high degree of homology exists
between pairs of genes from viruses of similar geographic origin. The
nucleotide sequences within a group differ by 1.5 to 10.6%; in contrast,
between groups the differences range from 15.8 to 19.4%. An evolutionary tree
for the nine sequences suggests that North American isolates have diverged
extensively from those circulating in other parts of the world. Geographic barriers
which determine flyway outlay may prevent the gene pools from extensive mixing.
The lack of correlation between date of isolation and evolutionary distance
suggests that different H4 HA genes cocirculate in a fashion similar to avian
H3 HA genes (H. Kida et al., 1987, Virology 159, 109-119) and influenza C genes
(D. Buonagurio et al., 1985, Virology 146, 221-232) implying the absence of
selective pressure by antibody that would give a significant advantage to
antigenic variants. In contrast to avian influenza virus genes, human influenza
virus genes evolve rapidly under the selective pressure of antibody.
Descriptors: hemagglutinins viral genetics, influenza A
virus genetics, amino acid sequence, base sequence, cloning, molecular,
geography, molecular sequence data, sequence homology, nucleic acid.
Dotti, C.G., J. Kartenbeck, and K. Simons (1993). Polarized
distribution of the viral glycoproteins of vesicular stomatitis, fowl plague
and Semliki Forest viruses in hippocampal neurons in culture: a light and
electron microscopy study. Brain Research 610(1): 141-7. ISSN: 0006-8993.
Abstract: We have shown previously using
immunofluorescence microscopy that upon infection of polarized hippocampal
cells in culture with vesicular stomatitis virus (VSV) and fowl plague virus
(FPV) the VSV glycoprotein is delivered to the plasma membrane of the dendrites
and of the cell body whereas the FPV hemagglutinin is transported to the axonal
surface (Cell, 62 (1990) 63-72). In this work electron microscopy of infected rat
hippocampal neurons showed that VSV progeny budded from the plasma membrane of
the dendrites and the cell body. The location of the budding virions
corresponded to the distribution of the VSV glycoprotein which was detected
over the somatodendritic plasma membrane by immunoelectron microscopy. In
contrast, no FPV formation was seen in the infected neurons although the FPV
hemagglutinin was localized to the axonal surface by immunoelectron microscopy.
In Semliki Forest virus (SFV) infected hippocampal cells we observed that the
viral glycoproteins were exclusively present in the dendrites and cell body but
not in axons.
Descriptors: cell polarity physiology, hippocampus
microbiology, membrane glycoproteins analysis, neurons microbiology, viral
envelope proteins analysis, cultured cells, hippocampus cytology, influenza A
virus avian isolation and purification, microscopy, microscopy, electron,
microscopy, immunoelectron, rats, rats, Sprague Dawley, Semliki Forest virus
isolation and purification, vesicular stomatitis Indiana virus isolation and
purification.
Dotti, C.G. and K. Simons (1990). Polarized
sorting of viral glycoproteins to the axon and dendrites of hippocampal neurons
in culture. Cell 62(1): 63-72.
ISSN: 0092-8674.
NAL
Call Number: QH573.C42
Abstract: Cultured hippocampal neurons were infected
with a temperature-sensitive mutant of vesicular stomatitis virus (VSV) and a
wild-type strain of the avian influenza fowl plague virus (FPV). The
intracellular distribution of viral glycoproteins was monitored by
immunofluorescence microscopy. In mature, fully polarized neurons the VSV
glycoprotein (a basolateral protein in epithelial MDCK cells) moved from the
Golgi complex to the dendritic domain, whereas the hemagglutinin protein of FPV
(an apically sorted protein in MDCK cells) was targeted preferentially, but not
exclusively, to the axon. The VSV glycoprotein appeared in clusters on the
dendritic surface, while the hemagglutinin was distributed uniformly along the
axonal membrane. Based on the finding that the same viral glycoproteins are
sorted in a polarized fashion in both neuronal and epithelial cells, we propose
that the molecular mechanisms of surface protein sorting share common features
in the two cell types.
Descriptors: axons microbiology, dendrites microbiology,
glycoproteins analysis, hippocampus microbiology, influenza A virus avian
genetics, neurons microbiology, vesicular stomatitis Indiana virus genetics,
viral proteins analysis, cultured cells, embryo, fluorescent antibody
technique, glycoproteins genetics, rats, viral proteins genetics.
Dragun, M., B. Rada, L. Novotny, and J. Beranek
(1990). Antiviral activities of pyrimidine nucleoside analogues: some
structure--activity relationships. Acta Virologica 34(4): 321-9
. ISSN: 0001-723X.
NAL
Call Number: 448.3 AC85
Abstract: Seventeen nucleoside derivatives (derived
from arabinosylcytosine, resp. cytidine, 5-fluorouracil and uracil) were tested
by agar-diffusion plaque-inhibition test for their antiviral activity with
herpes simplex, vaccinia, fowl plague, Newcastle disease and western equine
encephalomyelitis viruses. The highest antiviral activity against DNA viruses
exhibited arabinosylcytosine, N4-acylarabinosylcytosines, arabinosylthiouracil,
cyclocytidine and its 5'-chloroderivative. RNA viruses were inhibited by
5-fluorouridine only, whereas other tested compounds were ineffective or
showing marginal activity only. By search for relationship between chemical
structure and antiviral activity a tendency was found of higher antiviral
activity at lower lipophilicity. This is probably due to better transport of
the studied compounds into cell. The chemical structure, however, is the main
reason of antiviral activity.
Descriptors: antiviral agents chemistry, pyrimidine
nucleosides pharmacology, encephalitis virus, western equine drug effects,
encephalitis virus, western equine growth and development, influenza A virus
avian drug effects, avian growth and development, Newcastle disease virus drug
effects, Newcastle disease virus growth and development, plaque assay,
pyrimidine nucleosides chemistry, simplexvirus drug effects, simplexvirus
growth and development, structure activity relationship, vaccinia virus drug
effects, vaccinia virus growth and development.
Drzeniek, R. and A. Gauhe (1970). Differences in
substrate specificity of myxovirus neuraminidases. Biochemical and
Biophysical Research Communications 38(4): 651-6. ISSN: 0006-291X.
NAL
Call Number: 442.8 B5236
Descriptors: influenza A virus avian enzymology,
neuraminidase, Newcastle disease virus enzymology, binding sites, chromosomes,
genetic code, glycosides, kinetics, lactose, neuraminic acids, species
specificity, time factors.
Duc Dodon, M., R. Cecchelli, R. Cacan, L. Gazzolo,
and A. Verbert (1984). Viral neuraminidase and cellular
ectosialyltransferase in human lymphoblastoid cells infected with influenza
virus. Biochimie 66(6):
493-6. ISSN: 0300-9084.
NAL
Call Number: 383 SO1
Abstract: In human lymphoblastoid cells, infected with
an influenza virus, Fowl Plague Virus (FPV), glycoproteins (such as secreted
IgM) are hyposialylated, through the action of viral neuraminidase. In this
study, the modulation of the cellular ectosialyltransferase activity during
viral infection was investigated. This activity was detectable in FPV-infected
cells, was shown to be 2.5-fold higher than that of uninfected cells, and to be
able to restore, at least partially, the level of sialylation of the cell
surface acceptors.
Descriptors: cell transformation, viral, influenza A virus
avian enzymology, neuraminidase metabolism, sialyltransferases metabolism,
transferases metabolism, cell line, cell membrane metabolism, clostridium
enzymology, glycoproteins metabolism, kinetics, lymphocytes, membrane proteins
metabolism.
Duc Dodon, M., L. Gazzolo, G.A. Quash, and T.F. Wild
(1982). Secretion of immunoglobulins by human lymphocytes after infection
with influenza virus. Journal of General Virology 63(2):
441-50. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Abstract: The biosynthesis of IgM by the Epstein-Barr
virus-negative RAMOS lymphoblastoid cell line infected with an influenza A
virus, fowl plague virus Dobson strain (FPV-B), was investigated. The results
show that FPV infection of RAMOS cells slightly inhibited overall cellular
protein synthesis only at 24 h after infection, despite the synthesis of
FPV-specific proteins. However, even at this time, the synthesis and secretion
of IgM were not affected by virus infection. Secreted IgM contained a reduced
amount of sialic acid. The quantity of the asialylated IgM increased
proportionally to the amount of enzymically active neuraminidase, suggesting
that the asialylation of IgM is due to the action of virus neuraminidase. No
such asialylated IgM was observed in RAMOS cells infected with measles virus,
which does not possess neuraminidase. These results, together with a previous
observation of ours that asialylated immunoglobulins acquire an altered
antigenicity, suggest that the modulation of enzyme activities in B lymphocytes
in response to an exogenous aggression may lead to disturbances in the
structure and in the antigenic properties of immunoglobulins.
Descriptors: immunoglobulin m metabolism, influenza A
virus avian physiology, lymphocytes microbiology, cell line, immunoglobulin m
analysis, lymphocytes immunology, lymphoma, neuraminidase metabolism, proteins
analysis, sialic acids analysis, virus replication.
Duhaut, S.D. and J.W. McCauley (1996). Defective
RNAs inhibit the assembly of influenza virus genome segments in a
segment-specific manner. Virology 216(2): 326-337. ISSN: 0042-6822.
NAL
Call Number: 448.8 V81
Abstract: Four avian influenza viruses have been
generated, each containing a single extra defective RNA segment in addition to
the eight standard segments. Three of the extra RNAs were derived from segment
1 and the fourth from segment 2. Chick embryo fibroblast cells were infected
with each virus, and a wild-type virus. Virus RNA was quantified in extracts of
virus-infected cells and in virus released by 10 hr postinfection using reverse
transcription and by Northern blot analysis. In the case of two of the viruses
the presence of the defective RNA did not markedly affect the accumulation of
virus RNA within the infected cell, but significantly and selectively reduced
the amount of the "parent" segment in released virus. This effect was
reduced in a third virus. In a fourth virus, defective RNA was found to be
present at a low-input multiplicity and results were varied. Mixed infections of
one of the viruses with a closely related wild-type virus resulted in reduction
of the corresponding vRNA segment of the nondefective virus. We conclude that
assembly of influenza virus segments is not a purely random process.
Descriptors: chicks, avian influenza virus, RNA,
infection, pathogenesis, quantitative analysis, fibroblasts, acids, analytical
methods, birds, cells, chickens, disease transmission, domestic animals,
domesticated birds, Galliformes, influenza virus, livestock, nucleic acids, nucleic
compounds, organic acids, orthomyxoviridae, pathogenesis, poultry, useful
animals, viruses, young animals, reverse transcription, virus assembly,
transcription, mixed infections.
Durand, D.P. and R. Borland (1969). Effect of
input multiplicity on infection of cells with myxoviruses as studies by
hemadsorption. Proceedings of the Society for Experimental Biology and
Medicine, New York, NY 130(1): 44-7.
ISSN: 0037-9727.
NAL
Call Number: 442.9 So1
Descriptors: orthomyxoviridae pathogenicity, serologic
tests, hemadsorption inhibition tests, immune sera pharmacology, influenza A
virus avian pathogenicity, methods, Newcastle disease virus pathogenicity,
tissue culture.
Easterday, B., W.G. Laver, H.G. Pereira, and G.C.
Schild (1969). Antigenic composition of recombinant virus strains produced
from human and avian influenza A viruses. Journal of General Virology
5(1): 83-91. ISSN: 0022-1317.
NAL
Call Number: QR360.A1J6
Descriptors: antigens analysis, neuraminidase analysis,
orthomyxoviridae analysis, orthomyxoviridae immunology, recombination, genetic,
electrophoresis, hemagglutination inhibition tests, hemagglutinins viral
analysis, hybridization, genetic, immunodiffusion, influenza A virus avian.
Eggert, H.J., B. Brux, G. Righter, and H. Sinnecker
(1984). Charakterisierung der RNS-polymerase-aktivitat hochgereinigter
praparationen des influenzavirus a/duck/alberta/48/76. [Characterization of RNA
polymerase activity of highly purified preparations of influenza virus
A/duck/Alberta/48/76]. Zentralblatt Fur Bakteriologie, Mikrobiologie,
Und Hygiene. Series A, Medical Microbiology, Infectious Diseases, Virology,
Parasitology 256(4): 534-40. ISSN:
0176-6724.
NAL
Call Number: 448.3 C33 (1)
Abstract: The influenza virus A/duck/Alberta/48/76 with
the antigen formula H7N3 (16) and Hav1 Nav2 (WHO nomenclature from 1971) (15),
respectively, as well as a nonpathogenic virus of the subtype Hav1 were
purified to a high degree by ultracentrifugation in continuous sucrose
gradients (15-40% w/w and 20-60% w/w, respectively). The activity of the RNA
polymerase of this virus preparation was determined by incorporating 3H-UMP in
acid insoluble material following preincubation of the virus with the nonionic
detergens Nonidet P-40 for 15 min at 32 degrees C. The influence of different
concentrations was investigated of dinucleotid, NaCl, MgCl2, Nonidet P-40 and
different incubation temperatures. Optimal incorporation rates were found at
following conditions: 0.2 mM dinucleotid ApG, 150 mM sodium chloride and 8 mM
magnesium chloride by concentration of ions, 0.25-0.5% detergens Nonidet P-40
as well as a temperature of incubation of 32 degrees C. The data for optimal
polymerase activity for the avian influenza virus A/duck/Alberta/48/76 are
generally not different from the conditions described for the Fowl-Plague-Virus
and for human strains.
Descriptors: DNA directed RNA polymerases metabolism,
influenza A virus avian enzymology, bacteriological techniques, chick embryo,
enzyme activation, temperature.
Ehrhardt, C., C. Kardinal, W.J. Wurzer, T. Wolff, C.
von Eichel Streiber, S. Pleschka, O. Planz, and S. Ludwig (2004). Rac1 and
PAK1 are upstream of IKK-epsilon and TBK-1 in the viral activation of
interferon regulatory factor-3. FEBS Letters 567(2-3): 230-8. ISSN: 0014-5793.
NAL
Call Number: QD415.F4
Abstract: The anti-viral type I interferon (IFN)
response is initiated by the immediate induction of IFN beta, which is mainly
controlled by the IFN-regulatory factor-3 (IRF-3). The signaling pathways
mediating viral IRF-3 activation are only poorly defined. We show that the Rho
GTPase Rac1 is activated upon virus infection and controls IRF-3
phosphorylation and activity. Inhibition of Rac1 leads to reduced IFN beta
promoter activity and to enhanced virus production. As a downstream mediator of
Rac signaling towards IRF-3, we have identified the kinase p21-activated kinase
(PAK1). Furthermore, both Rac1 and PAK1 regulate the recently described IRF-3
activators, I kappa B kinase- and TANK-binding kinase-1, establishing a first canonical
virus-induced IRF-3 activating pathway.