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Review
. 2008 Mar;197(1):1-8.
doi: 10.1007/s00430-007-0055-0. Epub 2007 Jul 19.

Heat shock proteins: linking danger and pathogen recognition

Anke Osterloh  1 , Minka Breloer
Affiliations
Review

Heat shock proteins: linking danger and pathogen recognition

Anke Osterloh et al. Med Microbiol Immunol. 2008 Mar.

Abstract

Besides their central function in protein folding and transport within the cell, heat shock proteins (HSP) have been shown to modulate innate and adaptive immune response: (1) HSP mediate uptake and MHC presentation of HSP-associated peptides by antigen-presenting cells (APC). (2) HSP function as endogenous danger signals indicating cell stress and tissue damage to the immune system. (3) HSP bind pathogen-associated molecular pattern (PAMP) molecules and modulate PAMP-induced Toll-like receptor (TLR) signaling. Thus, HSP contribute to both, recognition of "danger" defined as uncontrolled tissue destruction and recognition of dangerous "nonself". In this review these different aspects of immune stimulation by HSP will be discussed.

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