Hepatitis A virus suppresses RIG-I-mediated IRF-3 activation to block induction of beta interferon

J Virol. 2005 Sep;79(17):10968-77. doi: 10.1128/JVI.79.17.10968-10977.2005.

Abstract

Hepatitis A virus (HAV) antagonizes the innate immune response by inhibition of double-stranded RNA (dsRNA)-induced beta interferon (IFN-beta) gene expression. In this report, we show that this is due to an interaction of HAV with the intracellular dsRNA-induced retinoic acid-inducible gene I (RIG-I)-mediated signaling pathway upstream of the kinases responsible for interferon regulatory factor 3 (IRF-3) phosphorylation (TBK1 and IKKepsilon). In consequence, IRF-3 is not activated for nuclear translocation and gene induction. In addition, we found that HAV reduces TRIF (TIR domain-containing adaptor inducing IFN-beta)-mediated IRF-3 activation, which is part of the Toll-like receptor 3 signaling pathway. As IRF-3 is necessary for IFN-beta transcription, inhibition of this factor results in efficient suppression of IFN-beta synthesis. This ability of HAV seems to be of considerable importance for HAV replication, as HAV is not resistant to IFN-beta, and it may allow the virus to establish infection and preserve the sites of virus production in later stages of the infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases
  • DNA-Binding Proteins / metabolism*
  • Hepatitis A / immunology*
  • Hepatitis A / metabolism
  • Hepatitis A virus / growth & development
  • Hepatitis A virus / pathogenicity*
  • Humans
  • I-kappa B Kinase
  • Interferon Regulatory Factor-3
  • Interferon-beta / antagonists & inhibitors*
  • Interferon-beta / genetics
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / metabolism
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism
  • Protein Structure, Tertiary
  • RNA Helicases / metabolism*
  • Receptors, Cell Surface / chemistry
  • Receptors, Cell Surface / metabolism
  • Receptors, Immunologic
  • Signal Transduction*
  • Toll-Like Receptor 3
  • Toll-Like Receptors
  • Transcription Factors / metabolism*
  • Transcription, Genetic

Substances

  • DNA-Binding Proteins
  • IRF3 protein, human
  • Interferon Regulatory Factor-3
  • Membrane Glycoproteins
  • Receptors, Cell Surface
  • Receptors, Immunologic
  • TLR3 protein, human
  • Toll-Like Receptor 3
  • Toll-Like Receptors
  • Transcription Factors
  • Interferon-beta
  • Protein Serine-Threonine Kinases
  • TBK1 protein, human
  • CHUK protein, human
  • I-kappa B Kinase
  • IKBKB protein, human
  • IKBKE protein, human
  • RIGI protein, human
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases
  • RNA Helicases