REVIEW

Chaperonins in disease: mechanisms, models, and treatments

J C Ranford and B Henderson

Cellular Microbiology Research Group, Eastman Dental Institute, University College London, 256 Gray’s Inn Road, London WC1X 8LD, UK

Correspondence to:
Correspondence to:
Dr B Henderson, Cellular Microbiology Research Group, Eastman Dental Institute, University College London, 256 Gray’s Inn Road, London WC1X 8LD, UK;
B.Henderson{at}eastman.ucl.ac.uk

Chaperonins are oligomeric proteins that assist in the folding of nascent or denatured proteins. Bacterial chaperonins are strongly immunogenic and can cause tissue pathology. They have been implicated in infection, autoimmune disease, and idiopathic or multifactorial diseases, such as arthritis and atherosclerosis. Chaperonin 60 proteins are also involved in prion diseases. In the past few years, much progress has been made in unravelling the involvement of various bacterial and mammalian chaperonin 60 (Cpn 60 or hsp 60) proteins in such diseases, and in proposing mechanisms for their biological actions, although we are still some way from a full understanding of chaperonin action that might lead to immunotherapeutic approaches. This review focuses on the current knowledge of the roles of Cpn 60 in the pathology of infectious and immune diseases, and discusses models for the actions of this molecule. Some potential therapeutic strategies will also be reviewed.

Keywords: Cpn 60; heat shock protein; immunogen

Abbreviations: CCT, chaperonin containing TCP-1; Cpn, chaperonin; IL-1, interleukin 1; PAMPs, pathogen associated molecular patterns; PrP, prion protein; PrP^Sc, abnormal, pathogenic isoform of PrP; TLR, Toll-like receptor

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