5'-triphosphate-dependent activation of PKR by RNAs with short stem-loops

Science. 2007 Nov 30;318(5855):1455-8. doi: 10.1126/science.1147347.

Abstract

Molecular patterns in pathogenic RNAs can be recognized by the innate immune system, and a component of this response is the interferon-induced enzyme RNA-activated protein kinase (PKR). The major activators of PKR have been proposed to be long double-stranded RNAs. We report that RNAs with very limited secondary structures activate PKR in a 5'-triphosphate-dependent fashion in vitro and in vivo. Activation of PKR by 5'-triphosphate RNA is independent of RIG-I and is enhanced by treatment with type 1 interferon (IFN-alpha). Surveillance of molecular features at the 5' end of transcripts by PKR presents a means of allowing pathogenic RNA to be distinguished from self-RNA. The evidence presented here suggests that this form of RNA-based discrimination may be a critical step in mounting an early immune response.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Cell Line, Tumor
  • Chlorocebus aethiops
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases / metabolism
  • Enzyme Activation
  • Eukaryotic Initiation Factor-2 / metabolism
  • Humans
  • Immunity, Innate
  • Interferon-alpha / immunology
  • Interferon-alpha / metabolism
  • Interferon-beta / metabolism
  • Molecular Sequence Data
  • Nucleic Acid Conformation*
  • Phosphoric Monoester Hydrolases / metabolism
  • Polyphosphates / metabolism
  • RNA / chemistry
  • RNA / genetics
  • RNA / metabolism*
  • RNA, Double-Stranded / chemistry
  • RNA, Double-Stranded / genetics
  • RNA, Double-Stranded / metabolism*
  • Receptors, Immunologic
  • Transfection
  • Vero Cells
  • eIF-2 Kinase / metabolism*

Substances

  • Eukaryotic Initiation Factor-2
  • Interferon-alpha
  • Polyphosphates
  • RNA, Double-Stranded
  • Receptors, Immunologic
  • RNA
  • Interferon-beta
  • eIF-2 Kinase
  • Phosphoric Monoester Hydrolases
  • RIGI protein, human
  • DEAD Box Protein 58
  • DEAD-box RNA Helicases
  • triphosphoric acid