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Impact of HSP-Chaperoned Peptides on the MHC Class II-Dependent Presentation and Activation of CD4+ T Cells in Regard of Allo- and Autoantigens

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Part of the book series: Heat Shock Proteins ((HESP,volume 1))

Abstract

HSP70:peptide complexes have multiple impact on APCs and consequently on the stimulation of T cells. HSPs activate APCs (innate response) and facilitate presentation of chaperoned peptides via MHC class I and II molecules (adaptive response) followed by effective CTL and CD4+ T cell responses. Cross-presentation of MHC class I-restricted epitopes is well investigated, the role in MHC class II-restricted antigen-presentation remains less clear but it becomes more and more obvious that peptides chaperoned by eukaryotic as well as prokaryotic HSPs particularly of the 70 kDa family are involved in MHC II-restricted presentation. HSP70 molecules bind a wide variety of self- and foreign peptides in an ATP- and pH-dependent manner and resulting HSP:peptide complexes can access MHC class II loading compartments via different possible mechanisms. Pro- and eukaryotic HSP70 chaperones have been found to facilitate processing and presentation of MHC class II-restricted antigens resulting in enhanced CD4+ T cell activation in response to allo- and auto-antigens. Further investigating the role of HSP70 in MHC II-restricted antigen-presentation will be of particular interest for a better understanding of the pathogenesis of autoimmune disorders and CD4+ T helper cell mediated tumour recognition

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Haug, M., Dannecker, G.E., Holzer, U. (2007). Impact of HSP-Chaperoned Peptides on the MHC Class II-Dependent Presentation and Activation of CD4+ T Cells in Regard of Allo- and Autoantigens. In: Asea, A.A., Maio, A.D. (eds) Heat Shock Proteins: Potent Mediators of Inflammation and Immunity. Heat Shock Proteins, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-5585-0_17

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