Mutations in the Membrane-Proximal Region of the Influenza A Virus M2 Protein Cytoplasmic Tail Have Modest Effects on Virus Replication

被引：27

作者：

Stewart, Shaun M. ^{[1
,2
]}

Pekosz, Andrew ^{[1
]}

机构：

[1] Johns Hopkins Univ, W Harry Feinstone Dept Mol Microbiol & Immunol, Bloomberg Sch Publ Hlth, Baltimore, MD 21205 USA

[2] Washington Univ, Div Biol & Biomed Sci, St Louis, MO 63110 USA

来源：

JOURNAL OF VIROLOGY | 2011年 / 85卷 / 23期

关键词：

ION-CHANNEL ACTIVITY; CHOLESTEROL-BINDING; MATRIX PROTEIN; PROTON CHANNEL; M1; PROTEIN; PARTICLES; PALMITOYLATION; HEMAGGLUTININ; NEURAMINIDASE; CONTRIBUTES;

D O I：

10.1128/JVI.05970-11

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Influenza A virus encodes M2, a proton channel that has been shown to be important during virus entry and assembly. In order to systematically investigate the role of the membrane-proximal residues in the M2 cytoplasmic tail in virus replication, we utilized scanning and directed alanine mutagenesis in combination with transcomplementation assays and recombinant viruses. The membrane-proximal residues 46 to 69 tolerated numerous mutations, with little, if any, effect on virus replication, suggesting that protein structure rather than individual amino acid identity in this region may be critical for M2 protein function.

引用

页码：12179 / 12187

页数：9

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