Exonuclease domain of the Lassa virus nucleoprotein is critical to avoid RIG-I signaling and to inhibit the innate immune response

J Virol. 2014 Dec;88(23):13923-7. doi: 10.1128/JVI.01923-14. Epub 2014 Sep 24.

Abstract

Lassa virus (LASV), which causes a viral hemorrhagic fever, inhibits the innate immune response. The exonuclease (ExoN) domain of its nucleoprotein (NP) is implicated in the suppression of retinoic acid-inducible gene I (RIG-I) signaling. We show here that a LASV in which ExoN function has been abolished strongly activates innate immunity and that this effect is dependent on RIG-I signaling. These results highlight the key role of NP ExoN function in the immune evasion that occurs during LASV infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cells, Cultured
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases / metabolism
  • Exonucleases / immunology*
  • Exonucleases / metabolism
  • Humans
  • Immune Tolerance*
  • Immunity, Innate*
  • Lassa virus / immunology*
  • Lassa virus / physiology*
  • Nucleoproteins / immunology*
  • Nucleoproteins / metabolism
  • Receptors, Immunologic
  • Signal Transduction*

Substances

  • Nucleoproteins
  • Receptors, Immunologic
  • Exonucleases
  • RIGI protein, human
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases