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

P. D. Nagy, R. Y. Wang, J. Pogany, A. Hafren, K. Makinen

Research output: Contribution to journalReview articlepeer-review

148 Scopus citations

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.

Original languageEnglish
Pages (from-to)374-382
Number of pages9
JournalVirology
Volume411
Issue number2
DOIs
StatePublished - Mar 15 2011

Bibliographical note

Funding Information:
The authors apologize to those colleagues whose works were not cited due to page limitations. This work was supported by the National Science Foundation ( IOB-0517218 ), and NIH-NIAID to PDN and by the Acagemy of Finland ( 206870 ) to KM.

Keywords

  • Cyclophilins
  • Flock house virus
  • Heat shock proteins
  • Hepatitis C virus
  • Host factors
  • Hsp70
  • Immunophilins
  • RNA viruses
  • Tomato bushy stunt virus
  • Virus replication

ASJC Scopus subject areas

  • Virology

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