Abstract
Heat shock proteins (HSPs) are intracellular chaperone, some of which function as immune adjuvants as well as danger signals for immune system when released into extracellular milieu. These HSPs, along with their client polypeptides, are specifically bound by receptors on antigen presenting cells (APCs). This leads to APC differentiation along with delivery of the chaperoned peptides for cross-presentation to T cells. HSP-APC interactions occur through several receptors that mediate endocytosis or signal transduction. Most importantly, HSP associated antigens are forced to enter the cross-presentation pathway by APCs, resulting in CD8+ T cell activation. These unique features of HSPs for the generation of immune response will be discussed.
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