Characterisation of a Novel N-Linked General Glycosylation Pathway as a Tool for Glycoengineering

Glycosylation plays a central role in the modification of proteins, from viruses to mammalian cells. But the lack of appropriate modification systems in bacteria has meant it is impossible to produce novel glycoproteins for study in simple hosts such as E. coli, until now. <P>
We have identified a novel N-linked general glycosylation pathway (Cjpgl) in Campylobacter jejuni and transferred it into E. coli, to produce recombinant PEB3 that appears structurally identical to the native glycoprotein (Wacker et al Science 2002 p1790- 3). We propose to characterise the Cjpgl pathway and optimise the N-linked glycosylation process in E.coli, providing the basis for a unique tool for glycoengineering, with broad research and industrial applications.