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.