Activation of the IFN-inducible enzyme RNase L causes apoptosis of animal cells

Virology. 1997 Sep 29;236(2):354-63. doi: 10.1006/viro.1997.8719.

Abstract

The interferon (IFN)-induced enzyme RNase L produced by a recombinant vaccinia virus (VV) causes death of mammalian cells with morphological and biochemical characteristics of apoptosis. Coexpression of 2-5A-synthetase enhances apoptosis induced by RNase L Activation of endogenous RNase L by infection with a VV ts mutant (ts22) or with wild-type virus in the presence of the antipoxvirus drug isatin-beta-thiosemicarbazone, a treatment known to significantly increase the amount of double-stranded RNA late during infection, also causes pronounced apoptosis of infected cells. The effects observed with recombinant virus-derived RNase L or with the endogenous enzyme are specific, since apoptosis also occurs in cells derived from mice lacking the IFN-induced protein kinase (PKR). The apoptosis antagonist Bcl-2 prevents induction of cell death by RNase L activation. Apoptosis of mammalian cells by RNase L activation could be a mechanism mediating anticellular actions of IFN.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 2',5'-Oligoadenylate Synthetase / genetics
  • 2',5'-Oligoadenylate Synthetase / metabolism
  • Animals
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • Cell Line
  • Endoribonucleases / biosynthesis
  • Endoribonucleases / metabolism*
  • Enzyme Activation
  • Enzyme Induction / drug effects
  • Humans
  • Interferons / pharmacology*
  • Mice
  • Protein Kinases / metabolism
  • Proto-Oncogene Proteins c-bcl-2 / pharmacology
  • Recombination, Genetic
  • Vaccinia virus / enzymology
  • Vaccinia virus / genetics

Substances

  • Proto-Oncogene Proteins c-bcl-2
  • Interferons
  • Protein Kinases
  • 2',5'-Oligoadenylate Synthetase
  • Endoribonucleases
  • 2-5A-dependent ribonuclease