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致病性奈瑟菌的菌毛蛋白O-糖基化途径是一种将外膜亚硝酸还原酶AniA进行糖基化的通用系统。

The pilin O-glycosylation pathway of pathogenic Neisseria is a general system that glycosylates AniA, an outer membrane nitrite reductase.

作者信息

Ku S C, Schulz B L, Power P M, Jennings M P

机构信息

School of Molecular and Microbial Sciences, The University of Queensland, St. Lucia, Brisbane, Qld 4072, Australia.

出版信息

Biochem Biophys Res Commun. 2009 Jan 2;378(1):84-9. doi: 10.1016/j.bbrc.2008.11.025. Epub 2008 Nov 14.

Abstract

O-Glycosylation is emerging as a common posttranslational modification of surface exposed proteins in bacterial mucosal pathogens. In pathogenic Neisseria an O-glycosylation pathway modifies a single abundant protein, pilin, the subunit protein that forms pili. Here, we identify an additional outer membrane glycoprotein in pathogenic Neisseria, the nitrite reductase AniA, that is glycosylated in its C-terminal repeat region by the pilin glycosylation pathway. To our knowledge, this is the first report of a general O-glycosylation pathway in a prokaryote. We also show that AniA displays polymorphisms in residues that map to the surface of the protein. A frame-shift mutation abolishes AniA expression in 34% of Neisseria meningitidis strains surveyed, however, all Neisseria gonorrhoeae strains examined are predicted to express AniA, implying a crucial role for AniA in gonococcal biology.

摘要

O-糖基化正逐渐成为细菌黏膜病原体中表面暴露蛋白常见的翻译后修饰方式。在致病性奈瑟菌中,一种O-糖基化途径修饰一种单一的丰富蛋白——菌毛蛋白,即形成菌毛的亚基蛋白。在此,我们鉴定出致病性奈瑟菌中另一种外膜糖蛋白,亚硝酸还原酶AniA,它在其C端重复区域通过菌毛蛋白糖基化途径进行糖基化。据我们所知,这是原核生物中一般O-糖基化途径的首次报道。我们还表明,AniA在映射到蛋白质表面的残基中表现出多态性。在接受调查的34%的脑膜炎奈瑟菌菌株中,一个移码突变消除了AniA的表达,然而,所有检测的淋病奈瑟菌菌株预计都表达AniA,这意味着AniA在淋球菌生物学中起关键作用。

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