Inhibition of the OAS/RNase L pathway by viruses

Curr Opin Virol. 2015 Dec:15:19-26. doi: 10.1016/j.coviro.2015.07.002. Epub 2015 Jul 29.

Abstract

The OAS/RNase L system was one of the first characterized interferon effector pathways. It relies on the synthesis, by oligoadenylate synthetases (OAS), of short oligonucleotides that act as second messengers to activate the latent cellular RNase L. Viruses have developed diverse strategies to escape its antiviral effects. This underscores the importance of the OAS/RNase L pathway in antiviral defenses. Viral proteins such as the NS1 protein of Influenza virus A act upstream of the pathway while other viral proteins such as Theiler's virus L* protein act downstream. The diversity of escape strategies used by viruses likely stems from their relative susceptibility to OAS/RNase L and other antiviral pathways, which may depend on their host and cellular tropism.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • 2',5'-Oligoadenylate Synthetase / antagonists & inhibitors*
  • 2',5'-Oligoadenylate Synthetase / metabolism
  • Animals
  • Base Sequence
  • Endoribonucleases / antagonists & inhibitors*
  • Endoribonucleases / metabolism
  • Humans
  • RNA Viruses / genetics
  • RNA Viruses / metabolism*
  • Viral Nonstructural Proteins / metabolism
  • Viral Proteins / antagonists & inhibitors*
  • Viral Proteins / metabolism
  • Virus Diseases / enzymology*

Substances

  • INS1 protein, influenza virus
  • Viral Nonstructural Proteins
  • Viral Proteins
  • 2',5'-Oligoadenylate Synthetase
  • Endoribonucleases
  • 2-5A-dependent ribonuclease