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 Gorodezky, Lisa Miorin, Mirco Schmolke, Benjamin G. Hale, Adolfo García-Sastre

Research output: Contribution to journalArticle

39 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)12146-12151
Number of pages6
JournalJournal of Virology
Volume88
Issue number20
DOIs
StatePublished - 2014
Externally publishedYes

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H7N9 Subtype Influenza A Virus
amino acid substitution
Amino Acid Substitution
Orthomyxoviridae
Virulence
virulence
viruses
interferons
Interferons
antagonists
proteins
genetic polymorphism
Viruses
Gene Expression
gene expression
cells
influenza virus INS1 protein

ASJC Scopus subject areas

  • Immunology
  • Virology
  • Medicine(all)

Cite this

A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence. / Ayllon, Juan; Domingues, Patricia; Rajsbaum Gorodezky, Ricardo; Miorin, Lisa; Schmolke, Mirco; Hale, Benjamin G.; García-Sastre, Adolfo.

In: Journal of Virology, Vol. 88, No. 20, 2014, p. 12146-12151.

Research output: Contribution to journalArticle

Ayllon, Juan ; Domingues, Patricia ; Rajsbaum Gorodezky, Ricardo ; Miorin, Lisa ; Schmolke, Mirco ; Hale, Benjamin G. ; García-Sastre, Adolfo. / A single amino acid substitution in the novel H7N9 influenza a virus NS1 protein increases CPSF30 binding and virulence. In: Journal of Virology. 2014 ; Vol. 88, No. 20. pp. 12146-12151.
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