Viral interaction with molecular chaperones: role in regulating viral infection.
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 antiviral therapeutic strategies targeting the virus-chaperone interactions.
Xiao
Allen
A
The James Hogg iCAPTURE Centre for Cardiovascular and Pulmonary Research, Department of Pathology and Laboratory Medicine, Providence Heart and Lung Institute, St. Paul's Hospital, University of British Columbia, Vancouver, BC V6Z 1Y6, Canada.
Wong
Jerry
J
Luo
Honglin
H
D015967:Gene Expression Regulation, Viral; D018832:Molecular Chaperones / Q000378:metabolism*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D014777:Virus Diseases / Q000378:metabolism*; D014780:Viruses / Q000235:genetics / Q000378:metabolism*
D018832:Molecular Chaperones; D014764:Viral Proteins