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Viral interaction with molecular chaperones: role in regulating viral infection

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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 antiviral therapeutic strategies targeting the virus-chaperone interactions.

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Acknowledgments

This manuscript was supported by grants from the Heart and Stroke Foundation of British Columbia and Yukon (HL) and the Canadian Institutes of Health Research (HL). JW is a recipient of a Doctoral Traineeship from the CIHR.

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  1. 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, 1081 Burrard St., Vancouver, BC, V6Z 1Y6, Canada

    Allen Xiao, Jerry Wong & Honglin Luo

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Xiao, A., Wong, J. & Luo, H. Viral interaction with molecular chaperones: role in regulating viral infection. Arch Virol 155, 1021–1031 (2010). https://doi.org/10.1007/s00705-010-0691-3

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