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Structure and Function: Heat Shock Proteins and Adaptive Immunity¹

Department of Medicine, Cambridge Institute for Medical Research, Addenbrooke’s Hospital, Cambridge, United Kingdom

Heat shock proteins (HSPs) have been implicated in the stimulation and generation of both innate and adaptive immunity. The ability of HSPs to bind antigenic peptides and deliver them to APCs is the basis of the generation of peptide-specific T lymphocyte responses both in vitro and in vivo. The different HSP families are genetically and biochemically unrelated, and the structural basis of peptide binding and the dynamic models of ligand interaction are known only for some of the HSPs. We examine the contribution of HSP structure to its immunological functions and the potential "immunological repertoire" of HSPs as well as the use of biophysical techniques to quantify HSP-peptide interactions and optimize vaccine design. Although biochemical evidence for HSP-mediated endogenous processing of Ag has now emerged, the issue of whether HSP-peptide complexes act as physiological sources of Ag in cross-presentation is controversial. We assess the contribution of biochemical studies in this field.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ B.J. is funded by the Medical Research Council. P.J.L. is funded by the Wellcome Trust and holds a Lister Institute Research Prize.

² Address correspondence and reprint requests to Dr. Babak Javid, Department of Medicine, Cambridge Institute for Medical Research, Addenbrooke’s Hospital, Cambridge CB2 2XY, U.K. E-mail address: bj10001{at}cam.ac.uk

³ Current address: Immunology Program, Department of Microbiology, The Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597.

⁴ Abbreviations used in this paper: HSP, heat shock protein; NBD, nucleotide binding domain; SBD, substrate binding domain.

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