Amino acid substitutions V63I or A37S/I61T/V63I/V100A in the PA N-terminal domain increase the virulence of H7N7 influenza A virus

Sci Rep. 2016 Nov 25:6:37800. doi: 10.1038/srep37800.

Abstract

The PA N-terminal domain (PA-Nter) is essential for viral transcription and replication. Here we identified PA-Nter substitutions A37S, I61T, V63I and V100A in recently emerged avian influenza A viruses (IAVs) with potential effect on virus pathogenicity and/or host adaptation. We introduced the identified PA-Nter substitutions into avian H7N7 IAV by reverse genetics. Our results showed that single substitution V63I and combined substitutions, I61T/V63I and A37S/I61T/V63I/V100A (Mfour), significantly increased virus growth capacity in mammalian cells. Meanwhile, these substitutions conferred higher virus transcription/replication capacity by producing more mRNA, cRNA and vRNA. Consistently, the polymerase activity and the endonuclease activity were enhanced by these PA-Nter substitutions. Notably, substitutions V63I and Mfour strongly increased virus replication and virulence in mice. Collectively, our findings demonstrated that the PA-Nter substitutions V63I and Mfour enhanced IAV pathogenicity through modification of the polymerase activity and the endonuclease activity, which added to the evolving knowledge of IAV virulence determinants.

MeSH terms

  • Amino Acid Substitution*
  • Animals
  • Birds
  • Cells, Cultured
  • Humans
  • Influenza A Virus, H7N7 Subtype / genetics
  • Influenza A Virus, H7N7 Subtype / growth & development
  • Influenza A Virus, H7N7 Subtype / pathogenicity*
  • Influenza in Birds / virology*
  • Mice
  • RNA, Messenger / genetics
  • RNA, Viral / genetics
  • Viral Proteins / chemistry*
  • Virulence

Substances

  • RNA, Messenger
  • RNA, Viral
  • Viral Proteins