The PDZ-binding motif of the avian NS1 protein affects transmission of the 2009 influenza A(H1N1) virus

Biochem Biophys Res Commun. 2014 Jun 20;449(1):19-25. doi: 10.1016/j.bbrc.2014.04.132. Epub 2014 May 4.

Abstract

By nature of their segmented RNA genome, influenza A viruses (IAVs) have the potential to generate variants through a reassortment process. The influenza nonstructural (NS) gene is critical for a virus to counteract the antiviral responses of the host. Therefore, a newly acquired NS segment potentially determines the replication efficiency of the reassortant virus in a range of different hosts. In addition, the C-terminal PDZ-binding motif (PBM) has been suggested as a pathogenic determinant of IAVs. To gauge the pandemic potential from human and avian IAV reassortment, we assessed the replication properties of NS-reassorted viruses in cultured cells and in the lungs of mice and determined their transmissibility in guinea pigs. Compared with the recombinant A/Korea/01/2009 virus (rK09; 2009 pandemic H1N1 strain), the rK09/VN:NS virus, in which the NS gene was adopted from the A/Vietnam/1203/2004 virus (a human isolate of the highly pathogenic avian influenza H5N1 virus strains), exhibited attenuated virulence and reduced transmissibility. However, the rK09/VN:NS-PBM virus, harboring the PBM in the C-terminus of the NS1 protein, recovered the attenuated virulence of the rK09/VN:NS virus. In a guinea pig model, the rK09/VN:NS-PBM virus showed even greater transmission efficiency than the rK/09 virus. These results suggest that the PBM in the NS1 protein may determine viral persistence in the human and avian IAV interface.

Keywords: Influenza A virus; Interferon; NS1 protein; PDZ-binding motif; Transmission.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Birds
  • Female
  • Guinea Pigs
  • Humans
  • Influenza A Virus, H1N1 Subtype / physiology*
  • Influenza, Human / transmission*
  • Influenza, Human / virology*
  • Mice
  • Mice, Inbred BALB C
  • PDZ Domains*
  • Structure-Activity Relationship
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / metabolism*
  • Virus Activation / physiology
  • Virus Replication / physiology

Substances

  • INS1 protein, influenza virus
  • Viral Nonstructural Proteins