Endoribonuclease activities of porcine reproductive and respiratory syndrome virus nsp11 was essential for nsp11 to inhibit IFN-β induction

Mol Immunol. 2011 Jul;48(12-13):1568-72. doi: 10.1016/j.molimm.2011.03.004. Epub 2011 Apr 9.

Abstract

Previous studies have shown that PRRSV nsp11, which was an endoribonuclease, was an interferon antagonist, however, the mechanism that nsp11 inhibited IFN-β production was unclear. To explore whether the endoribonuclease was required for nsp11 to disrupt the IFN-β production, substitutions of the presumed catalytic histidine and lysine residues of nsp11 were introduced into plasmid pcDNA 3.1-FLAG. The results showed that mutation that inactivated endoribonuclease made nsp11 lose its ability to inhibit Poly(I:C)-induced IFN-β promoter activity. In conclusion, our present work indicated that the endoribonuclease activity of nsp11 was essential for nsp11 to inhibit the IFN-β induction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Substitution
  • Animals
  • Blotting, Western
  • Cell Line
  • Chlorocebus aethiops
  • Endoribonucleases / metabolism*
  • Genes, Reporter
  • Histidine / genetics
  • Interferon-beta / biosynthesis*
  • Interferon-beta / genetics
  • Lysine / genetics
  • Plasmids / genetics
  • Poly I-C / metabolism
  • Porcine respiratory and reproductive syndrome virus / genetics
  • Porcine respiratory and reproductive syndrome virus / metabolism*
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism*

Substances

  • Viral Nonstructural Proteins
  • Histidine
  • Interferon-beta
  • Endoribonucleases
  • Lysine
  • Poly I-C