Protein glycosylation in bacteria: sweeter than ever.
Investigations into bacterial protein glycosylation continue to progress rapidly. It is now established that bacteria possess both N-linked and O-linked glycosylation pathways that display many commonalities with their eukaryotic and archaeal counterparts as well as some unexpected variations. In bacteria, protein glycosylation is not restricted to pathogens but also exists in commensal organisms such as certain Bacteroides species, and both the N-linked and O-linked glycosylation pathways can modify multiple proteins. Improving our understanding of the intricacies of bacterial protein glycosylation systems should lead to new opportunities to manipulate these pathways in order to engineer glycoproteins with potential value as novel vaccines.
Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada. nothaft@ualberta.ca
Harald
H
Nothaft
Christine M
CM
Szymanski
D000818:Animals; D001419:Bacteria / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001439:Bacteroides / Q000235:genetics / Q000378:metabolism; D016123:Campylobacter jejuni / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity; D020564:Deltaproteobacteria / Q000235:genetics / Q000378:metabolism; D020565:Epsilonproteobacteria / Q000235:genetics / Q000378:metabolism; D036781:Fimbriae Proteins / Q000737:chemistry / Q000378:metabolism; D016680:Genome, Bacterial; D006031:Glycosylation; D006801:Humans; D050356:Lipid Metabolism; D008954:Models, Biological; D009844:Oligosaccharides / Q000378:metabolism; D010802:Phylogeny
D001426:Bacterial Proteins; D009844:Oligosaccharides; D036781:Fimbriae Proteins