A. Graham Pockley

Stuart K. Calderwood

M. Gabriella Santoro

Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease provides the most current review of the literature relating to the role and influence of heat shock (stress) proteins on the establishment, progression and resolution of infectious disease. Written by leaders in the field of heat shock proteins (HSP) and their biological and immunological properties, the contributors provide a fascinating insight into the complex relationship between, and the involvement of prokaryotic and eukaryotic HSP in disease states. It has been known for some considerable time that heat shock proteins from prokaryotic organisms are immunodominant molecules that are intimately involved in the induction of potential protective inflammatory responses, and this aspect of HSP biology is updated herein. In addition to regulating heat shock protein gene expression, the transcription factor HSF1 also appears to play an important role in regulating immune responses to infection. Heat shock proteins are now known to influence infectious disease processes in a number of diverse ways: they are involved in the propagation of prions, the replication and morphogenesis of viruses, and the resistance of parasites to chemotherapy. These proteins also appear to be important mediators of bacteria-host interactions and inflammation, the latter via interactions with cell surface molecules and structures such as Toll-like receptors and lipid rafts. Heat shock proteins can be expressed on the surface of infected cells, and this is likely to provide a target for the innate immune response. Elevated levels of circulating HSP are present in infectious diseases and these proteins might therefore regulate inflammatory responses to pathogenic challenge on a systemic basis. Heat shock proteins are also implicated in the impact of genital tract infections on the reproductive outcome, as well as in the local and systemic consequences of periodontal disease. Fever-range temperatures can induce the expression of heat shock proteins, and the final chapter in the book examines the influence of fever-range hyperthermia on a variety of cells and the organization of plasma membranes. This book is an essential read for graduates and postgraduates in Biology, pro- and eukaryotic Biochemistry, Immunology, Microbiology, Inflammatory and Infectious Disease, and Pathology.

Prokaryotic and Eukaryotic Heat Shock Proteins in Infectious Disease

Brian Henderson

Since the beginning of the 21st Century there has been a rapid increase in our understanding of the cellular trafficking mechanisms of molecular chaperones in eukaryotes and in prokaryotes. In the former, molecular chaperone trafficking can occur between the various cellular compartments, with concomitant movement of other proteins. Such events can also result in the release of molecular chaperones from cells. In bacteria, molecular chaperones are involved in the trafficking of other proteins and are themselves released into the external milieu. The increasing appreciation of the role of molecular chaperones and Protein-Folding Catalysts in the interplay between bacteria and the cells of their hosts is now an important area of research for understanding the mechanisms of infectious diseases. This volume brings together experts in the biochemistry, cellular biology, immunology and molecular biology of molecular chaperones and Protein-Folding Catalysts with a focus on the mechanisms of cellular trafficking of these proteins and the role of these variegated trafficking mechanisms in both human and animal health and disease.

Cellular Trafficking of Cell Stress Proteins in Health and Disease

Originally published in 2005, this book reviews understanding of the biological roles of extracellular molecular chaperones. It provides an overview of the structure and function of molecular chaperones, their role in the cellular response to stress and their disposition within the cell. It also questions the basic paradigm of molecular chaperone biology - that these proteins are first and foremost protein-folding molecules. Paradigms of protein secretion are reviewed and the evolving concept of proteins (such as molecular chaperones) as multi-functional molecules for which the term 'moonlighting proteins' has been introduced is discussed. The role of exogenous molecular chaperones as cell regulators is examined and the physiological and pathophysiological role that molecular chaperones play is described. In the final section, the potential therapeutic use of molecular chaperones is described and the final chapter asks the question - what does the future hold for the extracellular biology of molecular chaperones?

A. Graham Pockley

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