Note: Intro -- Preface -- Contents -- Part I: Small Plant Heat Shock Proteins (HSP) -- Chapter 1: Small Heat Shock Proteins: Roles in Development, Desiccation Tolerance and Seed Longevity -- 1.1 Introduction -- 1.2 Small HSPs and Their Role in Development -- 1.2.1 Role of Small HSPs in Pollen Development -- 1.2.2 Role of Small HSPs in Seed Development -- 1.2.3 Role of Small HSPs During Seed Germination -- 1.2.4 Role of Small HSPs in Storage Organs -- 1.3 Molecular Regulation of Small HSP Accumulation During Development -- 1.4 Concerted Expression of Small HSPs with Other Seed Storage Proteins -- 1.5 Small HSPs: Key Players in Acquisition of Seed Desiccation Tolerance -- 1.6 Small HSPs Maintain Seed Viability During Aging -- 1.7 Small HSPs Impart Vigor and Better Germinability to Seeds Under Stress -- 1.8 Conclusion -- References -- Chapter 2: Plant Small Heat Shock Proteins and Its Interactions with Biotic Stress -- 2.1 Introduction -- 2.2 Plant HSP Family -- 2.3 General Role of HSP20 in Plant Defense Mechanism Against Biotic Stresses -- 2.4 Plant HSP20 in Immune Response During Bacteria Infection -- 2.5 HSP20 Activity in Plant Response Against Fungi -- 2.6 Plant HSP20 Associated to Nematodes Attack -- 2.7 HSP20 May Protect Plant Cells During Viral Infection -- 2.8 Conclusion -- References -- Chapter 3: Small Heat Shock Proteins, a Key Player in Grass Plant Thermotolerance -- 3.1 Introduction -- 3.2 Definition of sHSPS -- 3.3 Structure, Function and Regulation of SHSP -- 3.4 The Grass Family and the Mechanisms for Heat Tolerance -- 3.5 Identification and Characterization of SHSPS Associated with Heat Tolerance in Grasses -- 3.5.1 SHSPS Identified in Annual Species Cultivated as Grain Crops -- 3.6 SHSPS Identified in Perennial Species Cultivated as Forage or Turf Grasses -- 3.7 Conclusion -- References. , Chapter 4: Induction of Heat Shock Proteins During the Bud Dormancy Stage in Woody Fruit Plants -- 4.1 Introduction -- 4.2 Research Findings in Bud Dormancy of Woody Fruit Plants -- 4.3 Heat-Shock Proteins Detected During Bud Dormancy Stage -- 4.4 Role of Heat-Shock Proteins During the Bud Dormancy Stage -- 4.5 Conclusion -- References -- Chapter 5: Heat Shock Proteins in Wild Barley at "Evolution Canyon", Mount Carmel, Israel -- 5.1 Introduction -- 5.2 "Evolution Canyon" Model -- 5.3 Wild Barley, Hordeum spontaneum -- 5.4 Heat Shock Proteins (HSP) in Grasses -- 5.4.1 Small Heat Shock Proteins in Barley -- 5.5 HSP and Stress and Evolution -- 5.6 Barley HSP17 at Evolution Canyon -- 5.7 Future Studies on HSP at the "Evolution Canyon" Model -- 5.8 Conclusion -- References -- Chapter 6: Insights into the Mechanism of Heat Shock Mitigation Through Protein Repair, Recycling and Degradation -- 6.1 Introduction -- 6.2 Heat Shock Proteins as Molecular Chaperones -- 6.3 Heat Shock Factors -- 6.4 Regulation of Heat Shock Response -- 6.4.1 HSBP as HSF Regulator -- 6.4.2 BAG as Co-chaperones -- 6.5 Unfolded Protein Response and Autophagy -- 6.5.1 ATG6/Beclin1 Proteins -- 6.6 Recent Research Advances on HSR -- 6.7 Conclusion -- References -- Part II: Large Plant Heat Shock Proteins (HSP) -- Chapter 7: Plant Stress Response: Hsp70 in the Spotlight -- 7.1 Introduction -- 7.2 Hsp70 Function and Crosstalk in Plants -- 7.2.1 Hsp70 Chaperone Function and Regulation -- 7.2.2 Hsp70 in Growth and Development -- 7.2.3 Hsp70 as Translocator -- 7.2.4 Regulation of Induction of HSP70 - Heat Shock Response (HSR) -- 7.3 Multifaceted Role of HSP70 in Stress Tolerance of Plants -- 7.3.1 Biotic Stress Tolerance -- 7.3.2 Abiotic Stress Tolerance -- 7.3.3 Heat Stress -- 7.3.4 Drought Stress -- 7.3.5 Hsp70 in Abscisic Acid (ABA) Dependent Stress Signaling -- 7.3.6 Salinity Stress. , 7.3.7 Cold Stress -- 7.3.8 Flooding Stress -- 7.3.9 Inadequate or Excessive Light -- 7.3.10 Enhanced Concentrations of Heavy Metals -- 7.4 Combinatorial Stress and Hsp70 -- 7.5 Plant Stress Proteomics and Hsp70 -- 7.6 hsp70 Transgenics: The Road Ahead -- 7.7 Conclusion -- References -- Chapter 8: The Role of Plant 90-kDa Heat Shock Proteins in Plant Immunity -- 8.1 Introduction -- 8.2 Expression of HSP90 in Plants -- 8.3 HSP90 and the Plant Defense Response -- 8.4 HSP90 and Non-host Resistance -- 8.5 HSP90 and Host Resistance -- 8.6 Specific Requirement of HSP90 Isoforms by R Proteins -- 8.7 Conclusion -- References -- Chapter 9: Chloroplasts Heat Shock Protein 70B as Marker of Oxidative Stress -- 9.1 Introduction -- 9.2 Chloroplast HSP -- 9.3 Heat Shock Protein 70B (HSP70B) - Biomarker for Cell Resistance or Cell Susceptibility to Environmentally Induced Stress? -- 9.4 Conclusion -- 9.5 Genotype Resistance to Oxidative Stress and HSP70B Chaperone in Chlamydomonas Reinhardtii -- 9.6 How Organisms Cope with Oxidative Stress? -- 9.7 How Men Can Cope with Oxidative Stress in Plants? -- 9.8 What Approach Should Be Used to Obtain Fast and Reliable Information? -- 9.9 Conclusion -- References -- Chapter 10: The Involvement of HSP70 and HSP90 in Tomato Yellow Leaf Curl Virus Infection in Tomato Plants and Insect Vectors -- 10.1 Introduction -- 10.2 TYLCV Infection Leads to Reorganization of PQC Elements Including HSP70 and HSP90 in Host Cells -- 10.2.1 TYLCV-Induced Aggregation in Plant and Insect Host Organisms -- 10.2.2 Interaction Between Cellular HSPs and TYLCV Proteins -- 10.2.2.1 Co-localization of Host HSP70 and TYLCV CP -- 10.2.2.2 Complexes Between HSPs and TYLCV Proteins -- 10.2.2.3 TYLCV Infection Causes the Re-localization of PQC Elements in Host Cells. , 10.3 Downregulation of HSP70 and HSP90 Expression/Activity Differently Affect TYLCV Accumulation in Tomatoes -- 10.4 TYLCV Infection Interferes with Plant Stress Response Through Modifications in the Availability of HSPs -- 10.4.1 Combined Heat and Viral Stresses Induce the Efficient Aggregation of the Cellular Chaperones HSP70 and HSP90 -- 10.4.2 TYLCV Downregulates Heat Stress Response in Infected Plants -- 10.5 Conclusion -- References -- Part III: Heat Shock Proteins and Plant Therapeutics -- Chapter 11: Heat Shock Proteins and Phytochemicals: Role in Human Health and Disease -- 11.1 Introduction -- 11.2 Oxidative Stress - Involved Ischemia/Reperfusion Injury -- 11.2.1 Antioxidant Effects of Phytochemicals: Role of Heat Shock Proteins -- 11.2.1.1 Caffeic Acid Phenethyl Ester (CAPE) -- 11.2.1.2 1-[2-Cyano-3,12-Dioxooleana-1,9(11)-Dien-28-Oyl]Imidazole (CDDO-Im) -- 11.3 Obesity and Related Disorders -- 11.3.1 Heat Shock Proteins in Obesity and Related Disorders -- 11.3.2 Role of HSPs in Phytochemical-Induced Anti-obesity Effects -- 11.3.2.1 Curcumin -- 11.3.2.2 Resveratrol -- 11.3.2.3 Naringin -- 11.3.2.4 Epigallocatechin-3-Gallate -- 11.4 Liver Health and Disease -- 11.4.1 Role of HSPs in Liver Repair and Regeneration -- 11.4.2 Role of HSPs in Liver Disease -- 11.4.2.1 HSPs in hepatocellular carcinoma (HCC) -- Dietary Pomegranate Emulsion -- Black Currant Phytoconstituents -- 11.4.2.2 HSPs in alcoholic steatohepatitis (ASH) -- 11.4.2.3 HSPs in fluoride induced hepatotoxicity -- Caffeic Acid -- 11.4.2.4 HSPs in CCl4-induced hepatotoxicity -- Wei Kang Su and Flavonoids -- 11.5 Conclusion -- References -- Chapter 12: The Induction of Drosophila Heat Shock Proteins by Plants That Can Extend Fly Lifespan -- 12.1 Introduction -- 12.2 Aging, Hormesis, and Heat Shock Proteins -- 12.2.1 Rhodiola rosea -- 12.2.2 Cinnamon -- 12.2.3 Rosa damascena. , 12.3 Other Anti-aging Plants and Plant Products -- 12.4 Conclusion -- References -- Chapter 13: Molecular Chaperones and HSPs in Sugarcane and Eucalyptus -- 13.1 Introduction -- 13.1.1 Protein Folding, Structure and Function -- 13.1.2 Molecular Chaperones and Heat Shock Proteins (HSPs) Are Part of the Protein Quality Control (PQC) System -- 13.1.3 Main Proteins Involved with Stress Response -- 13.1.4 Heat Shock Factor (HSF) -- 13.1.5 The HSP70/HSP90 System -- 13.1.6 HSP60/HSP10 -- 13.1.7 HSP100 and sHSP -- 13.2 Stress Response and Chaperones in Plants -- 13.2.1 Stress Response -- 13.2.2 Chaperone Genome Analysis and Gene Expression Pattern in Plants -- 13.2.3 Chaperone Genome Analysis and Gene Expression Pattern in Sugarcane and Eucalyptus -- 13.3 Functional and Structural Advances on Sugarcane Chaperones -- 13.3.1 HSP70 -- 13.3.2 HSP90 -- 13.3.3 HSP100 -- 13.3.4 sHSP -- 13.4 Final Remarks -- References -- Chapter 14: Role of Heat Shock Proteins in Improving Heat Stress Tolerance in Crop Plants -- 14.1 Introduction -- 14.2 Heat Shock Proteins (Hsps) -- 14.3 Small Heat Shock Proteins (sHsps) -- 14.4 Heat Shock Protein 70 (Hsp70) -- 14.5 Heat Shock Protein 90 (Hsp90) -- 14.6 Heat Shock Protein 100 (Hsp100) -- 14.7 Chaperonins -- 14.8 Heat Shock Transcription Factors (Hsfs) -- 14.9 Heat Shock Promoters -- 14.10 Signaling Molecules Involved in the Heat Stress Response -- 14.11 Genomic Approaches for Heat Stress Tolerance -- 14.12 Conclusion -- References -- Chapter 15: NGS-Based Expression Profiling of HSP Genes During Cold and Freeze Stress in Seabuckthorn (Hippophae rhamnoides L.) -- 15.1 Introduction -- 15.2 Heat Shock Proteins: Role Under Cold/Freeze Stress in Plants -- 15.2.1 Seabuckthorn: Cold and Freeze Stress Adapted Plant -- 15.3 Transcriptome Analysis: Abundance of Heat Shock Protein Genes in Seabuckthorn Transcriptome. , 15.4 Differential Expression of HSP Genes Under Cold and Freeze Stress in Seabuckthorn.

Note: Intro -- Preface -- References -- Contributors -- 1 Role of HSF1 in Infectious Disease -- 1.1 Introduction -- 1.2 The Basic Biology of HSF -- 1.2.1 Overview of HSF Structure and Function -- 1.2.2 Activation of HSF Trimerization and HSE Binding Capacity -- 1.2.3 HSF Transactivating Activity -- 1.2.4 Regulation of HSF by Covalent Modification and Heterologous Protein Binding -- 1.2.4.1 HSF Phosphorylation -- 1.2.4.2 Other Covalent Modifications of HSF -- 1.2.4.3 Heterologous Protein Interactions -- 1.3 Activation of HSF1 by Factors Associated with Infections -- 1.3.1 Activation of HSF-1 at Febrile-Range Temperatures -- 1.3.2 Activation of Heat Shock Signaling by Products of Infection -- 1.4 Alterations in Heat Shock Response During Infections -- 1.5 Consequences of HSF1 Activation During Infection -- 1.5.1 Other Biological Effects of HSF1 Activation -- 1.5.2 Heat Shock, Cellular Injury and Survival -- 1.6 Conclusion -- References -- 2 Propagating Prions: An Essential Role for Molecular Chaperones -- 2.1 Introduction What Is a Prion? -- 2.2 Yeast Prions Proving the Prion Hypothesis -- 2.3 Role of Molecular Chaperones in Yeast Prion Propagation -- 2.3.1 Hsp104 -- 2.3.2 Hsp70s -- 2.4 Role of Hsp70 Co-chaperones in Yeast Prion Propagation Direct and Indirect Effects -- 2.5 Relevance of Yeast Prions to Mammalian Prion Diseases -- 2.6 Conclusions -- References -- 3 Role of Heat Shock Proteins in Viral Infection -- 3.1 Introduction -- 3.2 Modulation of the Heat Shock Response During Viral Infection -- 3.3 How Do Viruses Activate the Heat Shock Response? -- 3.4 Which Is the Functional Significance of HSP Induction During Viral Infection? -- 3.4.1 Virus Entry -- 3.4.2 Uncoating -- 3.4.3 Viral Gene Expression -- 3.4.4 Genome Replication -- 3.4.5 Assembly of Viral Components and Virion Morphogenesis. , 3.5 Effect of Hyperthermia and HSR Modulators on Virus Replication -- 3.5.1 Hsp90 Inhibitors and Virus Replication -- 3.5.2 Hyperthermia in Viral Infection -- 3.5.3 Induction of Heat Shock Proteins by Antiviral Agents -- 3.6 Concluding Remarks -- References -- 4 Chaperones in the Morphogenesis of Viruses -- 4.1 Introduction -- 4.2 Hsp60: Assisting Folding in Seclusion -- 4.2.1 The Hsp60 Chaperone Chamber -- 4.2.2 GroEL Interactions with Coats and Tails -- 4.2.3 TriC: A Bag of Tricks for Virus Assembly? -- 4.3 Hsp70: Assisting Folding by Local Interactions -- 4.3.1 The Hsp70 Chaperone Team -- 4.3.2 Hsp70 in Virion Assembly -- 4.3.3 Hsp70 in Disassembly -- 4.3.4 Hsp70 as Part of the Coat -- 4.4 Hsp90: Assisting Folding by Holding -- 4.4.1 The Hsp90 Chaperone Platform -- 4.4.2 Hsp90s in Viral Development -- 4.5 Concluding Remarks -- References -- 5 Role of Host Molecular Chaperones in Responses to Bacterial Infection and Endotoxin Exposure -- 5.1 Introduction -- 5.2 Heat Shock Proteins and Infection -- 5.3 Fever, Sepsis and the Anti-Inflammatory Influence of the HSR -- 5.4 Role of HSF1 and Heat Shock Proteins in Regulating NFB -- 5.5 Overriding the Heat Shock Response by Pro-inflammatory Signaling -- 5.6 Conclusions -- References -- 6 Mycobacterial Heat Shock Protein 60s in the Induction and Regulation of Infectious Disease -- 6.1 Introduction -- 6.2 Mycobacterial Hsp60s -- 6.2.1 Mycobacterial Diseases -- 6.2.2 Pathology of Tuberculosis -- 6.3 Immune Responses Against Mycobacteria and Mycobacterial Cpn60s -- 6.3.1 Mycobacteria, as well as Mycobacterial Cpn60s -- 6.3.2 Antibody Responses to Cpn60s -- 6.3.3 Cellular Responses to Cpn60s and Cytokine Release -- 6.4 The Role of Hsp60 in the Pathology of Tuberculosis -- 6.5 Protective and Misdirected Immune Responses Against Mycobacterial Cpn60 Proteins. , 6.5.1 Cpn60-Based Vaccines Against Mycobacterial Diseases -- 6.5.2 Regulation of Autoimmunity by Cpn60 Proteins -- 6.5.3 Hypothesis: Granuloma Activation-Suppression Cycle -- References -- 7 Heat Shock Proteins in Protozoan Parasites Leishmania spp. -- 7.1 The Organism -- 7.1.1 Gene Regulation in Leishmania spp. : A Farewell to Promoters -- 7.1.2 Leishmania Life Cycle and Pathogeny -- 7.1.3 Axenic Differentiation In Vitro -- 7.2 Heat Shock Proteins in Leishmania -- 7.2.1 The Heat Shock Protein Complement of Leishmania -- 7.2.2 Heat Shock Proteins and the Heat Shock Response -- 7.2.3 Stage-Specific Expression of Heat Shock Proteins in Leishmania -- 7.2.3.1 Pre-genome Era -- 7.2.3.2 Post-genome Era -- 7.3 Specific Roles in the Parasitic Life Cycle -- 7.3.1 Hsp100 -- 7.3.2 Hsp90 -- 7.3.3 Antogonistic roles for Hsp90 and Hsp100 -- 7.3.4 Heat Shock Proteins as Antigens in Leishmania Infections -- 7.3.5 Protection Against Anti-microbial Agents -- 7.4 Future Directions -- References -- 8 Toll-Like Receptors and Infectious Diseases: Role of Heat Shock Proteins -- 8.1 Introduction -- 8.2 Toll-Like Receptors Linked to Infectious Diseases -- 8.2.1 TLR1 -- 8.2.2 TLR2 -- 8.2.3 TLR3 -- 8.2.4 TLR4 -- 8.2.5 TLR5 -- 8.2.6 TLR6 -- 8.2.7 TLR7 and TLR8 -- 8.2.8 TLR9 -- 8.2.9 TLR11 -- 8.3 Conclusion -- References -- 9 Lipid Rafts, Lipopolysaccharide and Stress Proteins in Infectious Diseases -- 9.1 Introduction -- 9.2 Heat Shock Proteins as Intracellular Molecular Chaperones -- 9.3 Heat Shock Proteins as Extracellular Molecular Chaperones -- 9.4 Cell Surface Expression of Heat Shock Proteins -- 9.5 Lipid Rafts -- 9.6 Association of Heat Shock Proteins with Lipid Rafts -- 9.7 Role of Heat Shock Proteins in Acquired Immune Responses -- 9.8 Re-Presentation and Cross-Priming -- 9.9 Role of Heat Shock Protein in Innate Immune Responses. , 9.10 Lipopolysaccharide Recognition -- 9.11 Toll-Like Receptor Ligands? -- 9.12 Modulators of the Innate Immune Response? -- 9.13 Novel Therapeutic Interventions? -- 9.14 Concluding Remarks -- References -- 10 Heat Shock Proteins Are Mediators of Bacterial-HostInteractions -- 10.1 The Diversity of Life on Our Earth -- 10.1.1 Bacterial Diversity -- 10.1.1.1 Bacterial Diversity in Homo Sapiens -- 10.2 BacteriaHost Interactions -- 10.3 Heat Shock Proteins -- 10.3.1 Heat Shock Proteins as Moonlighting Proteins -- 10.4 Heat Shock Proteins and the Stress of Infection -- 10.5 Host Heat Shock Proteins Can Function as Receptors for Bacteria -- 10.6 Host Heat Shock Proteins Are Found in the Circulation: A New Homeostatic Network? -- 10.6.1 Signalling Actions of Host Heat Shock Proteins -- 10.7 Bacterial Heat Shock Proteins Are Virulence Factors? -- 10.7.1 Bacterial Molecular Chaperones Act as Bacterial Adhesins -- 10.7.2 Bacterial Molecular Chaperones as Directly Acting Virulence Factors -- 10.8 Bacterial Molecular Chaperones as Therapeutic Targets -- 10.9 Conclusions -- References -- 11 Membrane-Expressed and Extracellular Stress Proteins in Infectious Disease -- 11.1 Heat Shock Proteins (HSPs) -- 11.2 Membrane-Expressed and Extracellular Heat Shock Proteins Elicit Immune Responses -- 11.3 Microbial Infections -- 11.3.1 Escherichia coli ( E. coli ) -- 11.3.2 Salmonella typhimurium -- 11.3.3 Helicobacter pylori -- 11.3.4 Chlamydia pneumonia and Chlamydia trachomatis -- 11.3.5 Human Immunodeficiency Virus (HIV) -- 11.3.6 Epstein-Barr Virus (EBV) -- 11.3.7 Measles -- References -- 12 Circulating Stress Proteins in Infectious Disease -- 12.1 Introduction -- 12.2 Increase of Circulating Heat Shock Proteins During Infection -- 12.3 Origin of Circulating Heat Shock Proteins -- 12.4 Role of Circulating Heat Shock Proteins in Infection. , 12.5 Measurement of Circulating Heat Shock Proteins -- 12.6 Clinical Utility of Circulating Heat Shock Proteins Determinations -- 12.7 Conclusion -- References -- 13 Heat Shock Proteins, Genital Tract Infections and Reproductive Outcome -- 13.1 Infection-Related Heat Shock Protein Expression in the Female Genital Tract -- 13.1.1 Chlamydia trachomatis Infection -- 13.1.2 Vaginal Infections -- 13.1.3 Congenital Cytomegalovirus (CMV) Infection -- 13.2 Heat Shock Protein Expression During Pregnancy -- 13.2.1 Preimplantation Heat Shock Protein Expression -- 13.2.2 Influence of Antibodies to Heat Shock Proteins on Pre-implantation Embryo Development -- 13.2.3 Antibodies to Heat Shock Proteins and In Vitro Fertilisation -- 13.2.4 Heat Shock Proteins in Amniotic Fluid -- 13.2.5 Heat Shock Proteins as Biomarkers of Adverse Pregnancy Events -- 13.3 Polymorphisms in Heat Shock Protein Genes Influencing Pregnancy Outcome -- 13.4 Conclusions -- References -- 14 Heat Shock Proteins and Oral Diseases: Special Focuson Periodontitis -- 14.1 Gingivitis and Periodontitis -- 14.1.1 Etiology and Pathology -- 14.1.1.1 Gingivitis -- 14.1.1.2 Periodontitis -- 14.2 Heat Shock Proteins -- 14.2.1 Heat Shock Proteins and Atherosclerosis -- 14.2.2 Heat-Shock Proteins and Temporomandibular Joint Disorders -- 14.2.3 Heat Shock Proteins and Oral Mucosal Lesions -- 14.2.3.1 Oral Lichen -- References -- 15 Temperature Matters: Cellular Targets of Hyperthermia in Cancer Biology and Immunology -- 15.1 Introduction -- 15.2 Hyperthermia as a Radiosensitizer -- 15.3 Heat Shock Temperatures (4245C): Effects on Cell Structure and Morphology and the Plasma Membrane -- 15.3.1 Changes in Membrane Fluidity and Surface Morphology -- 15.3.2 Changes in Cytoskeletal Properties -- 15.3.3 Changes in Membrane Potential and Permeability. , 15.3.4 Changes in Plasma Membrane Association of Heat Shock and Other Proteins.

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