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Viral interaction with molecular chaperones: role in regulating viral infection

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Title: Viral interaction with molecular chaperones: role in regulating viral infection
Author: Luo, Honglin; Wong, Jerry; Xiao, Allen
Subject Keywords protein assembly;protein folding;virus infection;heat-shock protein;Chaperone
Issue Date: 2010-07-04
Publicly Available in cIRcle 2010-07-16
Publisher SpringerLink
Citation: Xiao, A., Wong, J., Luo, H. Viral interaction with molecular chaperones: role in regulating viral infection. Arch Virol. 2010; 155:1021–1031. DOI: 10.1007/s00705-010-0691-3. The original publication is available at www.springerlink.com.
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]
Affiliation: James Hogg iCAPTURE CentrePathology and Laboratory Medicine, Dept ofOther UBC
URI: http://hdl.handle.net/2429/26567
Peer Review Status: Reviewed
Scholarly Level: Researcher

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