Structure of the Newcastle disease virus F protein in the post-fusion conformation

被引：78

作者：

Swanson, Kurt ^{[2
,3
]}

Wen, Xiaolin ^{[1
]}

Leser, George P. ^{[2
]}

Paterson, Reay G. ^{[2
]}

Lamb, Robert A. ^{[2
,3
]}

Jardetzky, Theodore S. ^{[1
]}

机构：

[1] Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA

[2] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA

[3] Howard Hughes Med Inst, Chevy Chase, MD USA

来源：

VIROLOGY | 2010年 / 402卷 / 02期

基金：

美国国家卫生研究院;

关键词：

Paramyxovirus; Membrane fusion; Virus entry; Class I viral fusion proteins; NDV; PARAMYXOVIRUS FUSION PROTEIN; CRYSTAL-STRUCTURE; INFLUENZA HEMAGGLUTININ; EBOLA-VIRUS; CORE TRIMER; GLYCOPROTEIN; ECTODOMAIN; PREFUSION; SUBUNIT; GP2;

D O I：

10.1016/j.virol.2010.03.050

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The paramyxovirus F protein is a class I viral membrane fusion protein which undergoes a significant refolding transition during virus entry. Previous studies of the Newcastle disease virus, human parainfluenza virus 3 and parainfluenza virus 5 F proteins revealed differences in the pre- and post-fusion structures. The NDV Queensland (Q) F structure lacked structural elements observed in the other two structures, which are key to the refolding and fusogenic activity of F. Here we present the NDV Australia-Victoria (AV) F protein post-fusion structure and provide EM evidence for its folding to a pre-fusion form. The NDV AV F structure contains heptad repeat elements missing in the previous NDV QF structure, forming a post-fusion six-helix bundle (6HB) similar to the post-fusion hPIV3 F structure. Electrostatic and temperature factor analysis of the F structures points to regions of these proteins that may be functionally important in their membrane fusion activity. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：372 / 379

页数：8

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