Structure of an avian influenza A NS1 protein effector domain

BG Hale; WS Barclay; Richard Edward Randall; Rupert James Martin Russell

doi:10.1016/j.virol.2008.05.026

Structure of an avian influenza A NS1 protein effector domain

BG Hale, WS Barclay, Richard Edward Randall, Rupert James Martin Russell

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	1-5
Number of pages	5
Journal	Virology
Volume	378
DOIs	https://doi.org/10.1016/j.virol.2008.05.026
Publication status	Published - 15 Aug 2008

Keywords

avian influenza
NS1
X-ray crystallography
dimerization
interferon-antagonist
DOUBLE-STRANDED-RNA
BINDING
INTERFERON
SOFTWARE
SEQUENCE
PATHWAY

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@article{0f3f56b913c24ca3bbb14dac61afebc7,

title = "Structure of an avian influenza A NS1 protein effector domain",

abstract = "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.",

keywords = "avian influenza, NS1, X-ray crystallography, dimerization, interferon-antagonist, DOUBLE-STRANDED-RNA, BINDING, INTERFERON, SOFTWARE, SEQUENCE, PATHWAY",

author = "BG Hale and WS Barclay and Randall, \{Richard Edward\} and Russell, \{Rupert James Martin\}",

year = "2008",

month = aug,

day = "15",

doi = "10.1016/j.virol.2008.05.026",

language = "English",

volume = "378",

pages = "1--5",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press/Elsevier ",

}

TY - JOUR

T1 - Structure of an avian influenza A NS1 protein effector domain

AU - Hale, BG

AU - Barclay, WS

AU - Randall, Richard Edward

AU - Russell, Rupert James Martin

PY - 2008/8/15

Y1 - 2008/8/15

N2 - 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.

AB - 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.

KW - avian influenza

KW - NS1

KW - X-ray crystallography

KW - dimerization

KW - interferon-antagonist

KW - DOUBLE-STRANDED-RNA

KW - BINDING

KW - INTERFERON

KW - SOFTWARE

KW - SEQUENCE

KW - PATHWAY

UR - https://www.scopus.com/pages/publications/47749143963

U2 - 10.1016/j.virol.2008.05.026

DO - 10.1016/j.virol.2008.05.026

M3 - Article

SN - 0042-6822

VL - 378

SP - 1

EP - 5

JO - Virology

JF - Virology

ER -

Structure of an avian influenza A NS1 protein effector domain

Abstract

Keywords

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Virus NS1 - PI3 G0601126: Studies on the interaction of influenza virus NS1 protein with cellular P13-kinase

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Structure of an avian influenza A NS1 protein effector domain

Abstract

Keywords

Access to Document

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Projects

Virus NS1 - PI3 G0601126: Studies on the interaction of influenza virus NS1 protein with cellular P13-kinase

Cite this