Sensing viral RNAs by Dicer/RIG-I like ATPases across species

Curr Opin Immunol. 2015 Feb:32:106-13. doi: 10.1016/j.coi.2015.01.009. Epub 2015 Feb 3.

Abstract

Induction of antiviral immunity in vertebrates and invertebrates relies on members of the RIG-I-like receptor and Dicer families, respectively. Although these proteins have different size and domain composition, members of both families share a conserved DECH-box helicase domain. This helicase, also known as a duplex RNA activated ATPase, or DRA domain, plays an important role in viral RNA sensing. Crystallographic and electron microscopy studies of the RIG-I and Dicer DRA domains indicate a common structure and that similar conformational changes are induced by dsRNA binding. Genetic and biochemical studies on the function and regulation of DRAs reveal similarities, but also some differences, between viral RNA sensing mechanisms in nematodes, flies and mammals.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Animals
  • DEAD-box RNA Helicases / chemistry
  • DEAD-box RNA Helicases / metabolism*
  • Humans
  • Protein Binding
  • Protein Interaction Domains and Motifs
  • RNA, Viral / chemistry
  • RNA, Viral / metabolism*
  • Ribonuclease III / chemistry
  • Ribonuclease III / metabolism*
  • Virus Diseases / immunology*
  • Virus Diseases / metabolism*
  • Viruses / immunology*

Substances

  • RNA, Viral
  • Ribonuclease III
  • Adenosine Triphosphatases
  • DEAD-box RNA Helicases