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

J Virol. 2014 Oct;88(20):12146-51. doi: 10.1128/JVI.01567-14. Epub 2014 Jul 30.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Amino Acids / genetics*
  • Animals
  • Chickens
  • Gene Expression
  • Humans
  • Influenza A Virus, H7N9 Subtype / metabolism
  • Influenza A Virus, H7N9 Subtype / pathogenicity*
  • Influenza A Virus, H7N9 Subtype / physiology
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism*
  • Viral Proteins / metabolism*
  • Virulence

Substances

  • Amino Acids
  • INS1 protein, influenza virus
  • Viral Nonstructural Proteins
  • Viral Proteins