Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli

被引：71

作者：

Power, Peter M. ^{[1
]}

Seib, Kate L. ^{[1
]}

Jennings, Michael P. ^{[1
]}

机构：

[1] Univ Queensland, Sch Mol & Microbial Sci, Brisbane, Qld 4072, Australia

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 347卷 / 04期

基金：

英国医学研究理事会;

关键词：

Neisseria meningitidis; pilin; glycosylation; O-antigen ligase; pglL; wzy-dependent O-antigen biosynthesis;

D O I：

10.1016/j.bbrc.2006.06.182

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Pili (type IV fimbriae) of Neisseria meningitidis are glycosylated by the addition of O-linked sugars. Recent work has shown that PglF, a protein with homology to O-antigen 'flippases', is required for the biosynthesis of the pilin-linked glycan and suggests pilin glycosylation occurs in a manner analogous to the wzy-dependent addition of O-antigen to the core-LPS. O-Antigen ligases are crucial in this pathway for the transfer of undecraprenol-linked sugars to the LPS-core in Gram-negative bacteria. An O-antigen ligase homologue, pglL, was identified in N. meningitidis. PglL mutants showed no change in LPS phenotypes but did show loss of pilin glycosylation, confirming PglL is essential for pilin O-linked glycosylation in N. meningitidis. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：904 / 908

页数：5

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