Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease

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This book aims to explore the role of heat shock proteins in infectious disease. In bacterial infection, the host is encountered by the prokaryotic heat shock proteins expressed by microorganisms. These proteins tend to be made in large amounts as, pathogenic organisms suffer stresses such as heat shock and oxidative stress on entering the organs of their mammalian hosts. Although these proteins permit survival of the pathogen, they also are recognized as dominant antigens by the host which mounts an immune response largely targeted to the pathogens Hsp60 and Hsp70. This entails a certain amount of risk as the hsp are highly conserved - for instance human hsp70 is 50 per cent identical with the E. coli hsp70 called DNAK - autoimmunity is thus a risk. One of the themes of the book will be the contrasting effects of the mammalian and non-mammalian hsp on the immune response. These conserved molecules have both shared and differing effects on dendritic cells, B cells and T lymphocytes. We will examine in detail receptors for pro- and eukaryotic hsp and their immune and auto-immune response. These contrasting effects of pro- and eukaryotic hsp on immunity play a major role in auto-immune diseases such as rheumatoid arthritis. Recent date suggests that sequences in prokaryotic hsp60 are the important antigens in the development of RA. By contrast this can be modulated by immunoregulatory effects of mammalian hsp60 and 70. The hsp are also important in viral infections in which they require chaperone the large bursts of protein synthesis involved in viral replication and play a role in the effects on the viral promotors. Finally, hsp and heat shock factors play a key role in the resolution of the inflammation and fever and accompany infection. We will explore how hsp and HSF1 can regulate inflammatory transcription and cytokine and respond to the elevated temperatures of fever.