Antigenicity and irnmunogenicity of heat shock proteins

Abstract

Prokaryotic and eukaryotic organisms respond to potentially damaging stimuli such as elevated temperature by increasing the synthesis of a family of proteins collectively known as heat shock proteins (HSPs) or stress proteins. HSPs are among the most highly conserved and abundant proteins found in nature. Much interest has been generated in HSPs since they were described as dominant antigens of infectious microorganisms. It has been suggested that this immune recognition of pathogen HSPs serves as a first line of defense as well as a means by which autoimmune cascades may develop due to the inappropriate cross reactivity with self-HSPs. As a consequence of their chaperone functions, HSPs are associated with a broad spectrum of peptides derived from the cells from which they are isolated. Hence, it is not surprising that HSP-peptide complexes have been described as tumor specific antigens. Remarkably, it has been demonstrated that vaccination with these HSP-peptide complexes elicit protective immune response against the tumor from which complexes were isolated. Finally, recent findings indicate that the antigenic properties of HSPs can be exploited to enhance the humoral and cellular immune response to proteins of interest.