Open Collections

UBC Faculty Research and Publications

Viral interaction with molecular chaperones : role in regulating viral infection Luo, Honglin; Wong, Jerry; Xiao, Allen

Abstract

As essential effectors in protein quality control, molecular chaperones serve as the primary checkpoint to assist proper protein folding, and prevent misfolded proteins from denaturation and aggregation. In addition, chaperones can function to direct terminally-misfolded proteins to the proteolytic system for degradation. Viruses rely on host cell machineries for productive infection. Like for many other processes, various viruses have been shown to evolve mechanisms to utilize or subvert the host protein quality control machinery to support the completion of their life cycle. Furthermore, recent studies suggest that some viruses encode for their own chaperone-like proteins to enhance their infectivity. This review summarizes the current understanding of the interplay between molecular chaperones and viral proteins, highlights the chaperone activities of a number of viral proteins, and discusses potential anti-viral therapeutic strategies targeting the virus-chaperone interactions. [DOI: 10.1007/s00705-010-0691-3. The original publication is available at www.springerlink.com]

Item Metadata

Title
Viral interaction with molecular chaperones : role in regulating viral infection
Creator
Luo, Honglin; Wong, Jerry; Xiao, Allen
Contributor
James Hogg iCAPTURE Centre (University of British Columbia)
Publisher
SpringerLink
Date Issued
2010-07-04
Description
As essential effectors in protein quality control, molecular chaperones serve as the primary checkpoint to assist proper protein folding, and prevent misfolded proteins from denaturation and aggregation. In addition, chaperones can function to direct terminally-misfolded proteins to the proteolytic system for degradation. Viruses rely on host cell machineries for productive infection. Like for many other processes, various viruses have been shown to evolve mechanisms to utilize or subvert the host protein quality control machinery to support the completion of their life cycle. Furthermore, recent studies suggest that some viruses encode for their own chaperone-like proteins to enhance their infectivity. This review summarizes the current understanding of the interplay between molecular chaperones and viral proteins, highlights the chaperone activities of a number of viral proteins, and discusses potential anti-viral therapeutic strategies targeting the virus-chaperone interactions. [DOI: 10.1007/s00705-010-0691-3. The original publication is available at www.springerlink.com]
Subject
Protein assembly; Protein folding; Virus infection; Heat-shock protein; Chaperone
Genre
Article
Type
Text
Language
eng
Date Available
2011-07-04
Provider
Vancouver : University of British Columbia Library
Rights
Attribution-NonCommercial-NoDerivatives 4.0 International
DOI
10.14288/1.0048547
URI
http://hdl.handle.net/2429/26567
Affiliation
Pathology and Laboratory Medicine, Department of; Other UBC; Medicine, Faculty of
Citation
Xiao, A., Wong, J., Luo, H. Viral interaction with molecular chaperones: role in regulating viral infection. Arch Virol. 2010; 155:1021–1031.
Publisher DOI
10.1007/s00705-010-0691-3
Peer Review Status
Reviewed
Scholarly Level
Researcher; Faculty
Rights URI
http://creativecommons.org/licenses/by-nc-nd/4.0/
Aggregated Source Repository
DSpace

Item Media

Item Citations and Data

Rights

Attribution-NonCommercial-NoDerivatives 4.0 International