原核生物糖基化修饰系统及其应用前景  

Protein Glycosylation in Bacteria and its Application

作　　者：孙鹏[1] 马清钧[1] 吴军[1] 

机构地区：[1]军事医学科学院生物工程研究所,北京100071

出　　处：《生物技术通讯》2012年第2期262-266,共5页Letters in Biotechnology

摘　　要：传统认为只有真核生物才有蛋白质糖基化修饰现象,虽然在原核生物细胞中发现糖蛋白的存在已经有数十年,但是没有引起我们足够的重视。最近,在细菌中发现了蛋白质的糖基化修饰系统,最具代表性的是空肠弯曲弧菌的N-糖基化修饰系统、脑膜炎奈瑟球菌和绿脓杆菌的O-糖基化修饰系统。这些糖基化修饰系统已成功地转移到大肠杆菌中,并且独立发挥其糖基化修饰作用。寡糖转移酶在修饰过程中起关键作用,且寡糖转移酶对糖底物的特异性要求非常低,这使得按照我们的需求来"定制糖蛋白"成为可能,并标志着"原核生物糖基工程"的到来,这将为糖结合疫苗的发展提供良好的契机。Traditionally, protein glycosylation was considered to be limited to eukaryotes, however, through ad vances in analytical methods and genome sequencing, there have been increasing evidence of both Nlinked and 01inked protein glycosylation pathway in bacteria, for example, the Nlinked protein glycosylation system of Cam pylabacter jejuni and 01inked protein glycosylation system of Neisseria meningitides and Pseudomonas aeruginosct. Above all, the transfer of these glycosylation systerm to Escherichia coli and the low specific glycan substrate in the glycosylation reaction have enabled the production of recombinant glycoproteins. This has potentially provided the option for tailormade glycoproteins and has opened up the field of ＂prokaryote glycoengineering＂, especially the development of glycoconjugate vaccines.

关 键 词：糖基工程 蛋白糖基化 空肠弯曲弧菌 脑膜炎奈瑟球菌 绿脓杆菌 糖结合疫苗 

分 类 号：Q51[生物学—生物化学]