The cysteine protease domain of porcine reproductive and respiratory syndrome virus non-structural protein 2 antagonizes interferon regulatory factor 3 activation

J Gen Virol. 2010 Dec;91(Pt 12):2947-58. doi: 10.1099/vir.0.025205-0. Epub 2010 Sep 8.

Abstract

There is growing evidence that porcine reproductive and respiratory syndrome virus (PRRSV) has developed mechanisms to subvert the host innate immune response. PRRSV non-structural protein 2 (Nsp2) was suggested previously as a potential interferon (IFN) antagonist. This study focused on Nsp2 to investigate its inhibitory mechanism of IFN induction. It was demonstrated that Nsp2 strongly inhibited IFN-β production by antagonizing activation of the IFN regulatory factor 3 (IRF-3) pathway induced by the Sendai virus (SeV). Further studies revealed that the cysteine protease domain (PL2) of Nsp2 was necessary for IFN antagonism. Additionally, both full-length Nsp2 and the PL2 protease domain of Nsp2 were found to inhibit SeV-induced phosphorylation and nuclear translocation of IRF-3. These findings suggest that Nsp2 is likely to play an important role in subversion of IRF-3-dependent innate antiviral defences, providing a basis for elucidating the mechanisms underlying PRRSV pathogenesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Cysteine Endopeptidases / metabolism*
  • Humans
  • Interferon Regulatory Factor-3 / antagonists & inhibitors*
  • Interferon-beta / biosynthesis*
  • Porcine respiratory and reproductive syndrome virus / immunology*
  • Porcine respiratory and reproductive syndrome virus / pathogenicity*
  • Protein Structure, Tertiary
  • Sendai virus / immunology

Substances

  • Interferon Regulatory Factor-3
  • Interferon-beta
  • Cysteine Endopeptidases
  • nsP2 proteinase