Heat shock proteins in infection

Abstract

Heat shock proteins (HSPs) are constitutively expressed under physiological conditions in most organisms but their expression can significantly enhance in response to four types of stimuli including physical (e.g., radiation or heat shock), chemical and microbial (e.g., pathogenic bacteria, viruses, parasites and fungi) stimuli, and also dietary. These proteins were identified for their role in protecting cells from high temperature and other forms of stress. HSPs control physiological activities or virulence through interaction with various regulators of cellular signaling pathways. Several roles were determined for HSPs in the immune system including intracellular roles (e.g., antigen presentation and expression of innate receptors) as well as extracellular roles (e.g., tumor immunosurveillance and autoimmunity). It was observed that exogenously administered HSPs induced various immune responses in immunotherapy of cancer, infectious diseases, and autoimmunity. Moreover, virus interaction with HSPs as molecular chaperones showed important roles in regulating viral infections including cell entry and nuclear import, viral replication and gene expression, folding/assembly of viral protein, apoptosis regulation, and host immunity. Viruses could regulate host HSPs at different levels such as transcription, translation, post-translational modification and cellular localization. In this review, we attempt to overview the roles of HSPs in a variety of infectious diseases.

Keywords: Apoptosis; Chaperone; Heat shock protein; Immunity; Infectious disease.