Division of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK.
Biochem Soc Trans. 2010 Oct;38(5):1307-13. doi: 10.1042/BST0381307.
With glycosylation now firmly established across both Archaeal and bacterial proteins, a wide array of glycan diversity has become evident from structural analysis and genomic data. These discoveries have been built in part on the development and application of mass spectrometric technologies to the bacterial glycoproteome. This review highlights recent findings using high sensitivity MS of the large variation of glycans that have been reported on flagellin and pilin proteins of bacteria, using both 'top down' and 'bottom up' approaches to the characterization of these glycoproteins. We summarize current knowledge of the sugar modifications that have been observed on flagellins and pilins, in terms of both the diverse repertoire of monosaccharides observed, and the assemblage of moieties that decorate many of these sugars.
由于糖基化现在已在古菌和细菌蛋白质中得到充分证实，因此从结构分析和基因组数据中可以明显看出各种聚糖的多样性。这些发现部分基于质谱技术在细菌糖蛋白组学中的开发和应用。本综述重点介绍了使用高灵敏度 MS 技术对细菌鞭毛蛋白和菌毛蛋白上报道的大量聚糖进行的最新发现，这些聚糖的研究使用了“自上而下”和“自下而上”两种方法对这些糖蛋白进行了表征。我们总结了目前在鞭毛蛋白和菌毛蛋白上观察到的糖修饰的知识，包括观察到的单糖的多样化，以及许多这些糖上修饰基团的组合。
