A Single Amino Acid Substitution in the Novel H7N9 Influenza A Virus NS1 Protein Increases CPSF30 Binding and Virulence

被引：70

作者：

Ayllon, Juan ^{[1
]}

Domingues, Patricia ^{[4
]}

Rajsbaum, Ricardo ^{[1
]}

Miorin, Lisa ^{[1
]}

Schmolke, Mirco ^{[1
]}

Hale, Benjamin G. ^{[4
]}

Garcia-Sastre, Adolfo ^{[1
,2
,3
]}

机构：

[1] Icahn Sch Med Mt Sinai, Dept Microbiol, New York, NY 10029 USA

[2] Icahn Sch Med Mt Sinai, Dept Med, Div Infect Dis, New York, NY 10029 USA

[3] Icahn Sch Med Mt Sinai, Global Hlth & Emerging Pathogens Inst, New York, NY 10029 USA

[4] Univ Glasgow, MRC, Ctr Virus Res, Glasgow, Lanark, Scotland

来源：

JOURNAL OF VIROLOGY | 2014年 / 88卷 / 20期

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

RECEPTOR-BINDING; INTERFERON; REPLICATION; RECOGNITION; ABILITY;

D O I：

10.1128/JVI.01567-14

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Although an effective interferon antagonist in human and avian cells, the novel H7N9 influenza virus NS1 protein is defective at inhibiting CPSF30. An I106M substitution in H7N9 NS1 can restore CPSF30 binding together with the ability to block host gene expression. Furthermore, a recombinant virus expressing H7N9 NS1-I106M replicates to higher titers in vivo, and is subtly more virulent, than the parental virus. Natural polymorphisms in H7N9 NS1 that enhance CPSF30 binding may be cause for concern.

引用

页码：12146 / 12151

页数：6

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