Palmitoylation, pathogens and their host

被引：22

作者：

Blanc, Mathieu ^{[1
]}

Blaskovic, Sanja ^{[1
]}

van der Goot, F. Gisou ^{[1
]}

机构：

[1] Ecole Polytech Fed Lausanne, Global Hlth Inst, CH-1015 Lausanne, Switzerland

来源：

BIOCHEMICAL SOCIETY TRANSACTIONS | 2013年 / 41卷

基金：

瑞士国家科学基金会;

关键词：

bacterium; fungal pathogen; palmitoylation; parasite; pathogen; virus; PROTEIN PALMITOYLATION; MEMBRANE LOCALIZATION; BINDING; SPECIFICITY; ASSOCIATION; SEQUENCES; VIRULENCE; REVEALS; ALPHA;

D O I：

10.1042/BST20120337

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：

S-Palmitoylation, the only reversible post-translational lipid modification, confers unique biochemical and functional properties to proteins. Although it has long been known that viral proteins are palmitoylated, recent studies reveal that this modification plays a critical role for pathogens of all kinds and at multiple steps of their life cycle. The present review examines the involvement of S-palmitoylation in infection by viruses, bacteria and parasites and illustrates how pathogens have evolved to manipulate the host palmitoylation machinery.

引用

页码：84 / 88

页数：5

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