A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence

Juan Ayllon; Patricia Domingues; Ricardo Rajsbaum; Lisa Miorin; Mirco Schmolke; Benjamin G. Hale; Adolfo García-Sastre

doi:10.1128/JVI.01567-14

A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence

Juan Ayllon, Patricia Domingues, Ricardo Rajsbaum, Lisa Miorin, Mirco Schmolke, Benjamin G. Hale, Adolfo García-Sastre

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

45 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	12146-12151
Number of pages	6
Journal	Journal of virology
Volume	88
Issue number	20
DOIs	https://doi.org/10.1128/JVI.01567-14
State	Published - 2014
Externally published	Yes

ASJC Scopus subject areas

Microbiology
Immunology
Insect Science
Virology

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title = "A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence",

abstract = "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.",

author = "Juan Ayllon and Patricia Domingues and Ricardo Rajsbaum and Lisa Miorin and Mirco Schmolke and Hale, {Benjamin G.} and Adolfo Garc{\'i}a-Sastre",

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AU - Miorin, Lisa

AU - Schmolke, Mirco

AU - Hale, Benjamin G.

AU - García-Sastre, Adolfo

PY - 2014

Y1 - 2014

N2 - 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.

AB - 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.

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A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence

Abstract

ASJC Scopus subject areas

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