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

  • P. D. Nagy*
  • , R. Y. Wang
  • , J. Pogany
  • , A. Hafren
  • , K. Makinen
  • *Corresponding author for this work
  • University of Kentucky
  • University of Helsinki

Research output: Contribution to journalReview articlepeer-review

160 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 - 15 03 2011

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

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

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