Viral hijacking of cellular ubiquitination pathways as an anti-innate immunity strategy

被引：27

作者：

Chen, Mingzhou ^{[1
]}

Gerlier, Denis ^{[1
]}

机构：

[1] Univ Lyon 1, CNRS, UMR 5537, IFR Laennec,Lab Virol & Pathogenese Virale, F-69372 Lyon 08, France

来源：

VIRAL IMMUNOLOGY | 2006年 / 19卷 / 03期

关键词：

D O I：

10.1089/vim.2006.19.349

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Viruses are obligate parasites of host cells. Virus-host coevolution has selected virus for growth despite antiviral defenses set up by hosting cells and organisms. Ubiquitin conjugation onto proteins, through a cascade of reactions mediated by E1 (ubiquitin-activating enzyme) and E2 and E3 (ubiquitin-conjugating ligases), is one of the major regulatory systems that, in particular, tightly controls the concentration of cellular proteins by sorting them for degradation. The combined diversity of E2 and E3 ligases ensures the selective/specific ubiquitination of a large number of protein substrates within the cell interior. Therefore it is not surprising that several viruses encode proteins with E3 ubiquitin ligase activities that target cellular proteins playing a key role in innate antiviral mechanisms.

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页码：349 / 362

页数：14

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