Emerging picture of host chaperone and cyclophilin roles in RNA virus replication

Virology. 2011 Mar 15;411(2):374-82. doi: 10.1016/j.virol.2010.12.061. Epub 2011 Feb 3.

Abstract

Many plus-strand (+)RNA viruses co-opt protein chaperones from the host cell to assist the synthesis, localization and folding of abundant viral proteins, to regulate viral replication via activation of replication proteins and to interfere with host antiviral responses. The most frequently subverted host chaperones are heat shock protein 70 (Hsp70), Hsp90 and the J-domain co-chaperones. The various roles of these host chaperones in RNA virus replication are presented to illustrate the astonishing repertoire of host chaperone functions that are subverted by RNA viruses. This review also discusses the emerging roles of cyclophilins, which are peptidyl-prolyl isomerases with chaperone functions, in replication of selected (+)RNA viruses.

Publication types

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

MeSH terms

  • Cyclophilins / metabolism*
  • Host-Pathogen Interactions*
  • Molecular Chaperones / metabolism*
  • RNA Viruses / physiology*
  • Virus Replication*

Substances

  • Molecular Chaperones
  • Cyclophilins