Structure and function: Heat shock proteins and adaptive immunity

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 immunologicalfunctions and the potential immunological repertoire of HSPs as well as the use of biopbysical techniques to quantify HSP-peptide interactions and optimize vaccine design. Although biochemical evidence for HSP-mediated endogenousprocessing 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 biocbemical studies in this feild