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 journalArticle

41 Scopus citations


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
Issue number20
StatePublished - Jan 1 2014
Externally publishedYes


ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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