Structure of an avian influenza A virus NS1 protein effector domain

被引：81

作者：

Hale, Benjamin G. ^{[1
]}

Barclay, Wendy S. ^{[3
]}

Randall, Richard E. ^{[1
,2
]}

Russell, Rupert J. ^{[1
,2
]}

机构：

[1] Univ St Andrews, Ctr Biomol Sci, St Andrews KY16 9ST, Fife, Scotland

[2] Univ St Andrews, Interdisciplinary Ctr Human & Avian Influenza Res, St Andrews KY16 9ST, Fife, Scotland

[3] Univ London Imperial Coll Sci Technol & Med, Dept Virol, Fac Med, London W2 1PG, England

来源：

VIROLOGY | 2008年 / 378卷 / 01期

基金：

英国医学研究理事会;

关键词：

avian influenza; NS1; X-ray crystallography; dimerization; interferon-antagonist;

D O I：

10.1016/j.virol.2008.05.026

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Influenza A virus NS1 protein is a multifunctional virulence factor. Here, we report a crystal structure for the NS1 effector domain of avian influenza virus A/Duck/Albany/76. Comparison of this structure with that reported for a human strain shows both proteins share a common monomer conformation, albeit with subtle differences. Strikingly, our data reveal a novel helix-helix dimeric interface between monomers of the avian NS1 protein, which is also found in the human NS1 crystal lattice. We re-evaluate the current model of NS1 dimeric assembly, and provide biochemical evidence to show tryptophan-187 (a residue located at the helix-helix interface) is essential for dimerization of this effector domain. (c) 2008 Elsevier Inc. All rights reserved.

引用

页码：1 / 5

页数：5

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