Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada.
Nat Rev Microbiol. 2010 Nov;8(11):765-78. doi: 10.1038/nrmicro2383.
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.
对细菌蛋白质糖基化的研究仍在迅速进展。现在已经确定，细菌既具有 N 连接的糖基化途径，也具有 O 连接的糖基化途径，这些途径与真核生物和古菌的糖基化途径有许多共同之处，也有一些出人意料的差异。在细菌中，蛋白质糖基化不仅局限于病原体，也存在于共生生物中，如某些拟杆菌属物种，而且 N 连接和 O 连接的糖基化途径都可以修饰多种蛋白质。深入了解细菌蛋白质糖基化系统的复杂性，应该会为操纵这些途径提供新的机会，从而构建具有潜在价值的新型疫苗用糖蛋白。
