{"product_id":"moonlighting-proteins-9781118951118","title":"Moonlighting Proteins","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003ci\u003eMoonlighting Proteins: Novel Virulence Factors in Bacterial Infections\u003c\/i\u003e is a complete examination of the ways in which proteins with more than one unique biological action are able to serve as virulence factors in different bacteria.\u003c\/p\u003e \u003cp\u003eThe book explores the pathogenicity of bacterial moonlighting proteins, demonstrating the plasticity of protein evolution as it relates to protein function and to bacterial communication. Highlighting the latest discoveries in the field, it details the approximately 70 known bacterial proteins with a moonlighting function related to a virulence phenomenon. Chapters describe the ways in which each moonlighting protein can function as such for a variety of bacterial pathogens and how individual bacteria can use more than one moonlighting protein as a virulence factor. The cutting-edge research contained here offers important insights into many topics, from bacterial colonization, virulence, and antibiotic resistance, to protein structure and \u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003c\/p\u003e\u003cp\u003eList of Contributors xv\u003c\/p\u003e \u003cp\u003ePreface xix\u003c\/p\u003e \u003cp\u003eAbout the Editor xxiii\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart I Overview of Protein Moonlighting 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 What is Protein Moonlighting and Why is it Important? 3\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eConstance J. Jeffery\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 What is Protein Moonlighting? 3\u003c\/p\u003e \u003cp\u003e1.2 Why is Moonlighting Important? 5\u003c\/p\u003e \u003cp\u003e1.2.1 Many More Proteins Might Moonlight 5\u003c\/p\u003e \u003cp\u003e1.2.2 Protein Structure\/Evolution 5\u003c\/p\u003e \u003cp\u003e1.2.3 Roles in Health and Disease 8\u003c\/p\u003e \u003cp\u003e1.2.3.1 Humans 8\u003c\/p\u003e \u003cp\u003e1.2.3.2 Bacteria 10\u003c\/p\u003e \u003cp\u003e1.3 Current questions 11\u003c\/p\u003e \u003cp\u003e1.3.1 How Many More Proteins Moonlight? 11\u003c\/p\u003e \u003cp\u003e1.3.2 How Can We Identify Additional Proteins That Moonlight and all the Moonlighting Functions of Proteins? 11\u003c\/p\u003e \u003cp\u003e1.3.3 In Developing Novel Therapeutics, How Can We Target the Appropriate Function of a Moonlighting Protein and Not Affect Other Functions of the Protein? 12\u003c\/p\u003e \u003cp\u003e1.3.4 How do Moonlighting Proteins get Targeted to More Than One Location in the Cell? 12\u003c\/p\u003e \u003cp\u003e1.3.5 What Changes in Expression Patterns Have Occurred to Enable the Protein to be Available in a New Time and Place to Perform a New Function? 12\u003c\/p\u003e \u003cp\u003e1.4 Conclusions 13\u003c\/p\u003e \u003cp\u003eReferences 13\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Exploring Structure–Function Relationships in Moonlighting Proteins 21\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eSayoni Das, Ishita Khan, Daisuke Kihara, and Christine Orengo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 21\u003c\/p\u003e \u003cp\u003e2.2 Multiple Facets of Protein Function 22\u003c\/p\u003e \u003cp\u003e2.3 The Protein Structure–Function Paradigm 23\u003c\/p\u003e \u003cp\u003e2.4 Computational Approaches for Identifying Moonlighting Proteins 25\u003c\/p\u003e \u003cp\u003e2.5 Classification of Moonlighting Proteins 26\u003c\/p\u003e \u003cp\u003e2.5.1 Proteins with Distinct Sites for Different Functions in the Same Domain 27\u003c\/p\u003e \u003cp\u003e2.5.1.1 α‐Enolase, \u003ci\u003eStreptococcus pneumonia \u003c\/i\u003e27\u003c\/p\u003e \u003cp\u003e2.5.1.2 Albaflavenone monooxygenase, \u003ci\u003eStreptomyces coelicolor A\u003c\/i\u003e3\u003ci\u003e(\u003c\/i\u003e2\u003ci\u003e) \u003c\/i\u003e29\u003c\/p\u003e \u003cp\u003e2.5.1.3 MAPK1\/ERK2, \u003ci\u003eHomo sapiens \u003c\/i\u003e30\u003c\/p\u003e \u003cp\u003e2.5.2 Proteins with Distinct Sites for Different Functions in More Than One Domain 30\u003c\/p\u003e \u003cp\u003e2.5.2.1 Malate synthase\u003ci\u003e, Mycobacterium tuberculosis \u003c\/i\u003e31\u003c\/p\u003e \u003cp\u003e2.5.2.2 BirA, \u003ci\u003eEscherichia coli \u003c\/i\u003e31\u003c\/p\u003e \u003cp\u003e2.5.2.3 MRDI, \u003ci\u003eHomo sapiens \u003c\/i\u003e33\u003c\/p\u003e \u003cp\u003e2.5.3 Proteins Using the Same Residues for Different Functions 33\u003c\/p\u003e \u003cp\u003e2.5.3.1 GAPDH \u003ci\u003eE. coli \u003c\/i\u003e33\u003c\/p\u003e \u003cp\u003e2.5.3.2 Leukotriene A4 hydrolase, \u003ci\u003eHomo sapiens \u003c\/i\u003e33\u003c\/p\u003e \u003cp\u003e2.5.4 Proteins Using Different Residues in the Same\/Overlapping Site for Different Functions 34\u003c\/p\u003e \u003cp\u003e2.5.4.1 Phosphoglucose isomerase\u003ci\u003e, Oryctolagus cuniculus, Mus musculus, Homo sapiens \u003c\/i\u003e34\u003c\/p\u003e \u003cp\u003e2.5.4.2 Aldolase, \u003ci\u003ePlasmodium falciparum \u003c\/i\u003e36\u003c\/p\u003e \u003cp\u003e2.5.5 Proteins with Different Structural Conformations for Different Functions 36\u003c\/p\u003e \u003cp\u003e2.5.5.1 RfaH, \u003ci\u003eE. coli \u003c\/i\u003e36\u003c\/p\u003e \u003cp\u003e2.6 Conclusions 37\u003c\/p\u003e \u003cp\u003eReferences 39\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart II Proteins Moonlighting in Prokarya 45\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Overview of Protein Moonlighting in Bacterial Virulence 47\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eBrian Henderson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 47\u003c\/p\u003e \u003cp\u003e3.2 The Meaning of Bacterial Virulence and Virulence Factors 47\u003c\/p\u003e \u003cp\u003e3.3 Affinity as a Measure of the Biological Importance of Proteins 49\u003c\/p\u003e \u003cp\u003e3.4 Moonlighting Bacterial Virulence Proteins 50\u003c\/p\u003e \u003cp\u003e3.4.1 Bacterial Proteins Moonlighting as Adhesins 52\u003c\/p\u003e \u003cp\u003e3.4.2 Bacterial Moonlighting Proteins That Act as Invasins 59\u003c\/p\u003e \u003cp\u003e3.4.3 Bacterial Moonlighting Proteins Involved in Nutrient Acquisition 59\u003c\/p\u003e \u003cp\u003e3.4.4 Bacterial Moonlighting Proteins Functioning as Evasins 60\u003c\/p\u003e \u003cp\u003e3.4.5 Bacterial Moonlighting Proteins with Toxin‐like Actions 63\u003c\/p\u003e \u003cp\u003e3.5 Bacterial Moonlighting Proteins Conclusively Shown to be Virulence Factors 64\u003c\/p\u003e \u003cp\u003e3.6 Eukaryotic Moonlighting Proteins That Aid in Bacterial Virulence 66\u003c\/p\u003e \u003cp\u003e3.7 Conclusions 67\u003c\/p\u003e \u003cp\u003eReferences 68\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Moonlighting Proteins as Cross\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eReactive Auto\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eAntigens 81\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eWillem van Eden\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Autoimmunity and Conservation 81\u003c\/p\u003e \u003cp\u003e4.2 Immunogenicity of Conserved Proteins 82\u003c\/p\u003e \u003cp\u003e4.3 HSP Co‐induction, Food, Microbiota, and T-cell Regulation 84\u003c\/p\u003e \u003cp\u003e4.3.1 HSP as Targets for T‐Cell Regulation 85\u003c\/p\u003e \u003cp\u003e4.4 The Contribution of Moonlighting Virulence Factors to Immunological Tolerance 87\u003c\/p\u003e \u003cp\u003eReferences 88\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart III Proteins Moonlighting in Bacterial Virulence 93\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003ePart 3.1 Chaperonins: A Family of Proteins with Widespread Virulence Properties 95\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Chaperonin 60 Paralogs in \u003c\/b\u003e\u003ci\u003e\u003cb\u003eMycobacterium tuberculosis \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eand Tubercle Formation 97\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eBrian Henderson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 97\u003c\/p\u003e \u003cp\u003e5.2 Tuberculosis and the Tuberculoid Granuloma 97\u003c\/p\u003e \u003cp\u003e5.3 Mycobacterial Factors Responsible for Granuloma Formation 98\u003c\/p\u003e \u003cp\u003e5.4 \u003ci\u003eMycobacterium tuberculosis \u003c\/i\u003eChaperonin 60 Proteins, Macrophage Function, and Granuloma Formation 100\u003c\/p\u003e \u003cp\u003e5.4.1 \u003ci\u003eMycobacterium tuberculosis \u003c\/i\u003ehas Two Chaperonin 60 Proteins 100\u003c\/p\u003e \u003cp\u003e5.4.2 Moonlighting Actions of Mycobacterial Chaperonin 60 Proteins 101\u003c\/p\u003e \u003cp\u003e5.4.3 Actions of Mycobacterial Chaperonin 60 Proteins Compatible with the Pathology of Tuberculosis 102\u003c\/p\u003e \u003cp\u003e5.4.4 Identification of the Myeloid‐Cell‐Activating Site in \u003ci\u003eM. tuberculosis \u003c\/i\u003eChaperonin 60.1 105\u003c\/p\u003e \u003cp\u003e5.5 Conclusions 106\u003c\/p\u003e \u003cp\u003eReferences 106\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 \u003c\/b\u003e\u003ci\u003e\u003cb\u003eLegionella pneumophila \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eChaperonin 60, an Extra\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003e and Intra\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eCellular Moonlighting Virulence\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eRelated Factor 111\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eKarla N. Valenzuela\u003c\/i\u003e\u003ci\u003e‐\u003c\/i\u003e\u003ci\u003eValderas, Angela L. Riveroll, Peter Robertson, Lois E. Murray, and Rafael A. Garduno\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Background 111\u003c\/p\u003e \u003cp\u003e6.2 HtpB is an Essential Chaperonin with Protein‐folding Activity 112\u003c\/p\u003e \u003cp\u003e6.3 Experimental Approaches to Elucidate the Functional Mechanisms of HtpB 112\u003c\/p\u003e \u003cp\u003e6.3.1 The Intracellular Signaling Mechanism of HtpB in Yeast 113\u003c\/p\u003e \u003cp\u003e6.3.2 Yeast Two‐Hybrid Screens 118\u003c\/p\u003e \u003cp\u003e6.4 Secretion Mechanisms Potentially Responsible for Transporting HtpB to Extracytoplasmic Locations 120\u003c\/p\u003e \u003cp\u003e6.4.1 Ability of GroEL and HtpB to Associate with Membranes 121\u003c\/p\u003e \u003cp\u003e6.4.2 Ongoing Mechanistic Investigations on Chaperonins Secretion 122\u003c\/p\u003e \u003cp\u003e6.5 Identifying Functionally Important Amino Acid Positions in HtpB 124\u003c\/p\u003e \u003cp\u003e6.5.1 Site‐Directed Mutagenesis 125\u003c\/p\u003e \u003cp\u003e6.6 Functional Evolution of HtpB 126\u003c\/p\u003e \u003cp\u003e6.7 Concluding Remarks 127\u003c\/p\u003e \u003cp\u003eReferences 129\u003c\/p\u003e \u003cp\u003ePart 3.2 Peptidylprolyl Isomerases, Bacterial Virulence, and Targets for Therapy 135\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 An Overview of Peptidylprolyl Isomerases (PPIs) in Bacterial Virulence 137\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eBrian Henderson\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 137\u003c\/p\u003e \u003cp\u003e7.2 Proline and PPIs 137\u003c\/p\u003e \u003cp\u003e7.3 Host PPIs and Responses to Bacteria and Bacterial Toxins 138\u003c\/p\u003e \u003cp\u003e7.4 Bacterial PPIs as Virulence Factors 138\u003c\/p\u003e \u003cp\u003e7.4.1 Proposed Mechanism of Virulence of \u003ci\u003eLegionella pneumophila \u003c\/i\u003eMip 140\u003c\/p\u003e \u003cp\u003e7.5 Other Bacterial PPIs Involved in Virulence 140\u003c\/p\u003e \u003cp\u003e7.6 Conclusions 142\u003c\/p\u003e \u003cp\u003eReferences 142\u003c\/p\u003e \u003cp\u003ePart 3.3 Glyceraldehyde 3‐Phosphate Dehydrogenase (GAPDH): A Multifunctional Virulence Factor 147\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 GAPDH: A Multifunctional Moonlighting Protein in Eukaryotes and Prokaryotes 149\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMichael A. Sirover\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 149\u003c\/p\u003e \u003cp\u003e8.2 GAPDH Membrane Function and Bacterial Virulence 150\u003c\/p\u003e \u003cp\u003e8.2.1 Bacterial GAPDH Virulence 151\u003c\/p\u003e \u003cp\u003e8.2.2 GAPDH and Iron Metabolism in Bacterial Virulence 153\u003c\/p\u003e \u003cp\u003e8.3 Role of Nitric Oxide in GAPDH Bacterial Virulence 153\u003c\/p\u003e \u003cp\u003e8.3.1 Nitric Oxide in Bacterial Virulence: Evasion of the Immune Response 154\u003c\/p\u003e \u003cp\u003e8.3.2 Formation of GAPDH\u003csup\u003ecys\u003c\/sup\u003e\u003csup\u003e‐\u003c\/sup\u003e\u003csup\u003eNO\u003c\/sup\u003e by Bacterial NO Synthases 155\u003c\/p\u003e \u003cp\u003e8.3.3 GAPDH\u003csup\u003ecys\u003c\/sup\u003e\u003csup\u003e‐\u003c\/sup\u003e\u003csup\u003eNO\u003c\/sup\u003e in Bacterial Virulence: Induction of Macrophage Apoptosis 155\u003c\/p\u003e \u003cp\u003e8.3.4 GAPDH\u003csup\u003ecys\u003c\/sup\u003e\u003csup\u003e‐\u003c\/sup\u003e\u003csup\u003eNO\u003c\/sup\u003e in Bacterial Virulence: Inhibition of Macrophage iNOS Activity 156\u003c\/p\u003e \u003cp\u003e8.3.5 GAPDH\u003csup\u003ecys\u003c\/sup\u003e\u003csup\u003e‐\u003c\/sup\u003e\u003csup\u003eNO\u003c\/sup\u003e in Bacterial Virulence: Transnitrosylation to Acceptor Proteins 157\u003c\/p\u003e \u003cp\u003e8.4 GAPDH Control of Gene Expression and Bacterial Virulence 158\u003c\/p\u003e \u003cp\u003e8.4.1 Bacterial GAPDH Virulence 159\u003c\/p\u003e \u003cp\u003e8.5 Discussion 160\u003c\/p\u003e \u003cp\u003eAcknowledgements 162\u003c\/p\u003e \u003cp\u003eReferences 162\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 \u003c\/b\u003e\u003ci\u003e\u003cb\u003eStreptococcus pyogenes \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eGAPDH: A Cell\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eSurface Major Virulence Determinant 169\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eVijay Pancholi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction and Early Discovery 169\u003c\/p\u003e \u003cp\u003e9.2 GAS GAPDH: A Major Surface Protein with Multiple Binding Activities 170\u003c\/p\u003e \u003cp\u003e9.3 AutoADP‐Ribosylation of SDH and Other Post‐Translational Modifications 172\u003c\/p\u003e \u003cp\u003e9.4 Implications of the Binding of SDH to Mammalian Proteins for Cell Signaling and Virulence Mechanisms 173\u003c\/p\u003e \u003cp\u003e9.5 Surface Export of SDH\/GAPDH: A Cause or Effect? 178\u003c\/p\u003e \u003cp\u003e9.6 SDH: The GAS Virulence Factor‐Regulating Virulence Factor 180\u003c\/p\u003e \u003cp\u003e9.7 Concluding Remarks and Future Perspectives 183\u003c\/p\u003e \u003cp\u003eReferences 183\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Group B \u003c\/b\u003e\u003ci\u003e\u003cb\u003eStreptococcus \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eGAPDH and Immune Evasion 195\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003ePaula Ferreira and Patrick Trieu\u003c\/i\u003e\u003ci\u003e‐\u003c\/i\u003e\u003ci\u003eCuot\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 The Bacterium GBS 195\u003c\/p\u003e \u003cp\u003e10.2 Neonates are More Susceptible to GBS Infection than Adults 195\u003c\/p\u003e \u003cp\u003e10.3 IL‐10 Production Facilitates Bacterial Infection 196\u003c\/p\u003e \u003cp\u003e10.4 GBS Glyceraldehyde‐3‐Phosphate Dehydrogenase Induces IL‐10 Production 197\u003c\/p\u003e \u003cp\u003e10.5 Summary 199\u003c\/p\u003e \u003cp\u003eReferences 200\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 \u003c\/b\u003e\u003ci\u003e\u003cb\u003eMycobacterium tuberculosis \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eCell\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eSurface GAPDH Functions as a Transferrin Receptor 205\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eVishant M. Boradia, Manoj Raje, and Chaaya Iyengar Raje\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 205\u003c\/p\u003e \u003cp\u003e11.2 Iron Acquisition by Bacteria 206\u003c\/p\u003e \u003cp\u003e11.2.1 Heme Uptake 206\u003c\/p\u003e \u003cp\u003e11.2.2 Siderophore‐Mediated Uptake 207\u003c\/p\u003e \u003cp\u003e11.2.3 Transferrin Iron Acquisition 207\u003c\/p\u003e \u003cp\u003e11.3 Iron Acquisition by Intracellular Pathogens 207\u003c\/p\u003e \u003cp\u003e11.4 Iron Acquisition by \u003ci\u003eM. tb \u003c\/i\u003e208\u003c\/p\u003e \u003cp\u003e11.4.1 Heme Uptake 208\u003c\/p\u003e \u003cp\u003e11.4.2 Siderophore‐Mediated Iron Acquisition 209\u003c\/p\u003e \u003cp\u003e11.4.3 Transferrin‐Mediated Iron Acquisition 209\u003c\/p\u003e \u003cp\u003e11.5 Glyceraldehyde‐3‐Phosphate Dehydrogenase (GAPDH) 210\u003c\/p\u003e \u003cp\u003e11.6 Macrophage GAPDH and Iron Uptake 210\u003c\/p\u003e \u003cp\u003e11.6.1 Regulation 210\u003c\/p\u003e \u003cp\u003e11.6.2 Mechanism of Iron Uptake and Efflux 211\u003c\/p\u003e \u003cp\u003e11.6.3 Role of Post‐Translational Modifications 211\u003c\/p\u003e \u003cp\u003e11.7 Mycobacterial GAPDH and Iron Uptake 212\u003c\/p\u003e \u003cp\u003e11.7.1 Regulation 212\u003c\/p\u003e \u003cp\u003e11.7.2 Mechanism of Iron Uptake 215\u003c\/p\u003e \u003cp\u003e11.7.3 Uptake by Intraphagosomal \u003ci\u003eM. tb \u003c\/i\u003e216\u003c\/p\u003e \u003cp\u003e11.8 Conclusions and Future Perspectives 216\u003c\/p\u003e \u003cp\u003eAcknowledgements 218\u003c\/p\u003e \u003cp\u003eReferences 219\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 GAPDH and Probiotic Organisms 225\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eHideki Kinoshita\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Introduction 225\u003c\/p\u003e \u003cp\u003e12.2 Probiotics and Safety 225\u003c\/p\u003e \u003cp\u003e12.3 Potential Risk of Probiotics 227\u003c\/p\u003e \u003cp\u003e12.4 Plasminogen Binding and Enhancement of its Activation 228\u003c\/p\u003e \u003cp\u003e12.5 GAPDH as an Adhesin 229\u003c\/p\u003e \u003cp\u003e12.6 Binding Regions 232\u003c\/p\u003e \u003cp\u003e12.7 Mechanisms of Secretion and Surface Localization 234\u003c\/p\u003e \u003cp\u003e12.8 Other Functions 235\u003c\/p\u003e \u003cp\u003e12.9 Conclusion 236\u003c\/p\u003e \u003cp\u003eReferences 237\u003c\/p\u003e \u003cp\u003ePart 3.4 Cell‐Surface Enolase: A Complex Virulence Factor 245\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Impact of Streptococcal Enolase in Virulence 247\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMarcus Fulde and Simone Bergmann\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 247\u003c\/p\u003e \u003cp\u003e13.2 General Characteristics 248\u003c\/p\u003e \u003cp\u003e13.3 Expression and Surface Exposition of Enolase 249\u003c\/p\u003e \u003cp\u003e13.4 Streptococcal Enolase as Adhesion Cofactor 252\u003c\/p\u003e \u003cp\u003e13.4.1 Enolase as Plasminogen‐Binding Protein 252\u003c\/p\u003e \u003cp\u003e13.4.1.1 Plasminogen‐Binding Sites of Streptococcal Enolases 253\u003c\/p\u003e \u003cp\u003e13.4.2 Role of Enolase in Plasminogen‐Mediated Bacterial‐Host Cell Adhesion and Internalization 254\u003c\/p\u003e \u003cp\u003e13.4.3 Enolase as Plasminogen‐Binding Protein in Non‐Pathogenic Bacteria 255\u003c\/p\u003e \u003cp\u003e13.5 Enolase as Pro‐Fibrinolytic Cofactor 256\u003c\/p\u003e \u003cp\u003e13.5.1 Degradation of Fibrin Thrombi and Components of the Extracellular Matrix 257\u003c\/p\u003e \u003cp\u003e13.6 Streptococcal Enolase as Cariogenic Factor in Dental Disease 258\u003c\/p\u003e \u003cp\u003e13.7 Conclusion 258\u003c\/p\u003e \u003cp\u003eAcknowledgement 259\u003c\/p\u003e \u003cp\u003eReferences 259\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Streptococcal Enolase and Immune Evasion 269\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eMasaya Yamaguchi and Shigetada Kawabata\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 269\u003c\/p\u003e \u003cp\u003e14.2 Localization and Crystal Structure 271\u003c\/p\u003e \u003cp\u003e14.3 Multiple Binding Activities of α‐Enolase 273\u003c\/p\u003e \u003cp\u003e14.4 Involvement of α‐Enolase in Gene Expression Regulation 276\u003c\/p\u003e \u003cp\u003e14.5 Role of Anti‐α‐Enolase Antibodies in Host Immunity 277\u003c\/p\u003e \u003cp\u003e14.6 α‐Enolase as Potential Therapeutic Target 279\u003c\/p\u003e \u003cp\u003e14.7 Questions Concerning α‐Enolase 281\u003c\/p\u003e \u003cp\u003eReferences 281\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 \u003c\/b\u003e\u003ci\u003e\u003cb\u003eBorrelia burgdorferi \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eEnolase and Plasminogen Binding 291\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eCatherine A. Brissette\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction to Lyme Disease 291\u003c\/p\u003e \u003cp\u003e15.2 Life Cycle 292\u003c\/p\u003e \u003cp\u003e15.3 Borrelia Virulence Factors 292\u003c\/p\u003e \u003cp\u003e15.4 Plasminogen Binding by Bacteria 293\u003c\/p\u003e \u003cp\u003e15.5 \u003ci\u003eB. burgdorferi \u003c\/i\u003eand Plasminogen Binding 294\u003c\/p\u003e \u003cp\u003e15.6 Enolase 295\u003c\/p\u003e \u003cp\u003e15.7 \u003ci\u003eB. burgdorferi \u003c\/i\u003eEnolase and Plasminogen Binding 297\u003c\/p\u003e \u003cp\u003e15.8 Concluding Thoughts 301\u003c\/p\u003e \u003cp\u003eAcknowledgements 301\u003c\/p\u003e \u003cp\u003eReferences 301\u003c\/p\u003e \u003cp\u003ePart 3.5 Other Glycolytic Enzymes Acting as Virulence Factors 309\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Triosephosphate Isomerase from \u003c\/b\u003e\u003ci\u003e\u003cb\u003eStaphylococcus aureus \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eand Plasminogen Receptors on Microbial Pathogens 311\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eReiko Ikeda and Tomoe Ichikawa\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction 311\u003c\/p\u003e \u003cp\u003e16.2 Identification of Triosephosphate Isomerase on \u003ci\u003eS. aureus\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eas a Molecule that Binds to the Pathogenic Yeast \u003ci\u003eC. neoformans \u003c\/i\u003e312\u003c\/p\u003e \u003cp\u003e16.2.1 Co‐Cultivation of \u003ci\u003eS. aureus \u003c\/i\u003eand \u003ci\u003eC. neoformans \u003c\/i\u003e312\u003c\/p\u003e \u003cp\u003e16.2.2 Identification of Adhesins on \u003ci\u003eS. aureus \u003c\/i\u003eand \u003ci\u003eC. neoformans \u003c\/i\u003e312\u003c\/p\u003e \u003cp\u003e16.2.3 Mechanisms of \u003ci\u003eC. neoformans \u003c\/i\u003eCell Death 313\u003c\/p\u003e \u003cp\u003e16.3 Binding of Triosephosphate Isomerase with Human Plasminogen 314\u003c\/p\u003e \u003cp\u003e16.4 Plasminogen‐Binding Proteins on \u003ci\u003eTrichosporon asahii \u003c\/i\u003e314\u003c\/p\u003e \u003cp\u003e16.5 Plasminogen Receptors on \u003ci\u003eC. neoformans \u003c\/i\u003e316\u003c\/p\u003e \u003cp\u003e16.6 Conclusions 316\u003c\/p\u003e \u003cp\u003eReferences 317\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Moonlighting Functions of Bacterial Fructose 1,6\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eBisphosphate Aldolases 321\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eNeil J. Oldfield, Fariza Shams, Karl G. Wooldridge, and David P.J. Turner\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Introduction 321\u003c\/p\u003e \u003cp\u003e17.2 Fructose 1,6‐bisphosphate Aldolase in Metabolism 321\u003c\/p\u003e \u003cp\u003e17.3 Surface Localization of Streptococcal Fructose 1,6‐bisphosphate Aldolases 322\u003c\/p\u003e \u003cp\u003e17.4 Pneumococcal FBA Adhesin Binds Flamingo Cadherin Receptor 323\u003c\/p\u003e \u003cp\u003e17.5 FBA is Required for Optimal Meningococcal Adhesion to Human Cells 324\u003c\/p\u003e \u003cp\u003e17.6 \u003ci\u003eMycobacterium tuberculosis \u003c\/i\u003eFBA Binds Human Plasminogen 325\u003c\/p\u003e \u003cp\u003e17.7 Other Examples of FBAs with Possible Roles in Pathogenesis 326\u003c\/p\u003e \u003cp\u003e17.8 Conclusions 327\u003c\/p\u003e \u003cp\u003eReferences 327\u003c\/p\u003e \u003cp\u003ePart 3.6 Other Metabolic Enzymes Functioning in Bacterial Virulence 333\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Pyruvate Dehydrogenase Subunit B and Plasminogen Binding in \u003c\/b\u003e\u003ci\u003e\u003cb\u003eMycoplasma \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003e335\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eAnne Gründel, Kathleen Friedrich, Melanie Pfeiffer, Enno Jacobs, and Roger Dumke\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Introduction 335\u003c\/p\u003e \u003cp\u003e18.2 Binding of Human Plasminogen to \u003ci\u003eM. pneumoniae \u003c\/i\u003e337\u003c\/p\u003e \u003cp\u003e18.3 Localization of PDHB on the Surface of \u003ci\u003eM. pneumoniae \u003c\/i\u003eCells 340\u003c\/p\u003e \u003cp\u003e18.4 Conclusions 343\u003c\/p\u003e \u003cp\u003eReferences 344\u003c\/p\u003e \u003cp\u003ePart 3.7 Miscellaneous Bacterial Moonlighting Virulence Proteins 349\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 Unexpected Interactions of Leptospiral Ef\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eTu and Enolase 351\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eNatália Salazar and Angela Barbosa\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19.1 \u003ci\u003eLeptospira \u003c\/i\u003e–Host Interactions 351\u003c\/p\u003e \u003cp\u003e19.2 \u003ci\u003eLeptospira \u003c\/i\u003eEf‐Tu 352\u003c\/p\u003e \u003cp\u003e19.3 \u003ci\u003eLeptospira \u003c\/i\u003eEnolase 353\u003c\/p\u003e \u003cp\u003e19.4 Conclusions 354\u003c\/p\u003e \u003cp\u003eReferences 354\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 \u003c\/b\u003e\u003ci\u003e\u003cb\u003eMycobacterium tuberculosis \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003eAntigen 85 Family Proteins: Mycolyl Transferases and Matrix\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eBinding Adhesins 357\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eChristopher P. Ptak, Chih\u003c\/i\u003e\u003ci\u003e‐\u003c\/i\u003e\u003ci\u003eJung Kuo, and Yung\u003c\/i\u003e\u003ci\u003e‐\u003c\/i\u003e\u003ci\u003eFu Chang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20.1 Introduction 357\u003c\/p\u003e \u003cp\u003e20.2 Identification of Antigen 85 358\u003c\/p\u003e \u003cp\u003e20.3 Antigen 85 Family Proteins: Mycolyl Transferases 359\u003c\/p\u003e \u003cp\u003e20.3.1 Role of the Mycomembrane 359\u003c\/p\u003e \u003cp\u003e20.3.2 Ag85 Family of Homologous Proteins 359\u003c\/p\u003e \u003cp\u003e20.3.3 Inhibition and Knockouts of Ag85 360\u003c\/p\u003e \u003cp\u003e20.4 Antigen 85 Family Proteins: Matrix‐Binding Adhesins 361\u003c\/p\u003e \u003cp\u003e20.4.1 Abundance and Location 361\u003c\/p\u003e \u003cp\u003e20.4.2 Ag85 a Fibronectin‐Binding Adhesin 362\u003c\/p\u003e \u003cp\u003e20.4.3 Ag85 an Elastin‐Binding Adhesin 363\u003c\/p\u003e \u003cp\u003e20.4.4 Implication in Disease 364\u003c\/p\u003e \u003cp\u003e20.5 Conclusion 365\u003c\/p\u003e \u003cp\u003eAcknowledgement 365\u003c\/p\u003e \u003cp\u003eReferences 365\u003c\/p\u003e \u003cp\u003ePart 3.8 Bacterial Moonlighting Proteins that Function as Cytokine Binders\/Receptors 371\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 Miscellaneous IL\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003e1\u003c\/b\u003e\u003cb\u003eβ\u003c\/b\u003e\u003cb\u003e‐\u003c\/b\u003e\u003cb\u003eBinding Proteins of\u003c\/b\u003e\u003cb\u003e \u003c\/b\u003e\u003ci\u003e\u003cb\u003eAggregatibacter actinomycetemcomitans \u003c\/b\u003e\u003c\/i\u003e\u003cb\u003e373\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRiikka Ihalin\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e21.1 Introduction 373\u003c\/p\u003e \u003cp\u003e21.2 \u003ci\u003eA. actinomycetemcomitans \u003c\/i\u003eBiofilms Sequester IL‐1β 374\u003c\/p\u003e \u003cp\u003e21.3 \u003ci\u003eA. actinomycetemcomitans \u003c\/i\u003eCells Take in IL‐1β 375\u003c\/p\u003e \u003cp\u003e21.3.1 Novel Outer Membrane Lipoprotein of \u003ci\u003eA. actinomycetemcomitans \u003c\/i\u003eBinds IL‐1β 375\u003c\/p\u003e \u003cp\u003e21.3.2 IL‐1β Localizes to the Cytosolic Face of the Inner Membrane and in the Nucleoids of \u003ci\u003eA. actinomycetemcomitans \u003c\/i\u003e377\u003c\/p\u003e \u003cp\u003e21.3.3 Inner Membrane Protein ATP Synthase Subunit β Binds IL‐1β 377\u003c\/p\u003e \u003cp\u003e21.3.4 DNA‐Binding Histone‐Like Protein HU Interacts with IL‐1β 378\u003c\/p\u003e \u003cp\u003e21.4 The Potential Effects of IL‐1β on \u003ci\u003eA. actinomycetemcomitans \u003c\/i\u003e379\u003c\/p\u003e \u003cp\u003e21.4.1 Biofilm Amount Increases and Metabolic Activity Decreases 379\u003c\/p\u003e \u003cp\u003e21.4.2 Potential Changes in Gene Expression 380\u003c\/p\u003e \u003cp\u003e21.5 Conclusions 381\u003c\/p\u003e \u003cp\u003eReferences 382\u003c\/p\u003e \u003cp\u003ePart 3.9 Moonlighting Outside of the Box 387\u003c\/p\u003e \u003cp\u003e\u003cb\u003e22 Bacteriophage Moonlighting Proteins in the Control of Bacterial Pathogenicity 389\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJanine Z. Bowring, Alberto Marina, José R. Penadés, and Nuria Quiles\u003c\/i\u003e\u003ci\u003e‐\u003c\/i\u003e\u003ci\u003ePuchalt\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e22.1 Introduction 389\u003c\/p\u003e \u003cp\u003e22.2 Bacteriophage T4 I‐TevI Homing Endonuclease Functions as a Transcriptional Autorepressor 391\u003c\/p\u003e \u003cp\u003e22.3 Capsid Psu Protein of Bacteriophage P4 Functions as a Rho Transcription Antiterminator 394\u003c\/p\u003e \u003cp\u003e22.4 Bacteriophage Lytic Enzymes Moonlight as Structural Proteins 398\u003c\/p\u003e \u003cp\u003e22.5 Moonlighting Bacteriophage Proteins De‐Repressing Phage‐Inducible Chromosomal Islands 398\u003c\/p\u003e \u003cp\u003e22.6 dUTPase, a Metabolic Enzyme with a Moonlighting Signalling Role 401\u003c\/p\u003e \u003cp\u003e22.7 \u003ci\u003eEscherichia coli \u003c\/i\u003eThioredoxin Protein Moonlights with T7 DNA Polymerase for Enhanced T7 DNA Replication 404\u003c\/p\u003e \u003cp\u003e22.8 Discussion 404\u003c\/p\u003e \u003cp\u003eReferences 406\u003c\/p\u003e \u003cp\u003e\u003cb\u003e23 Viral Entry Glycoproteins and Viral Immune Evasion 413\u003c\/b\u003e\u003cb\u003e\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJonathan D. Cook and Jeffrey E. Lee\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e23.1 Introduction 413\u003c\/p\u003e \u003cp\u003e23.2 Enveloped Viral Entry 414\u003c\/p\u003e \u003cp\u003e23.3 Moonlighting Activities of Viral Entry Glycoproteins 415\u003c\/p\u003e \u003cp\u003e23.3.1 Viral Entry Glycoproteins Moonlighting as Evasins 416\u003c\/p\u003e \u003cp\u003e23.3.2 Evading the Complement System 417\u003c\/p\u003e \u003cp\u003e23.3.3 Evading Antibody Surveillance 419\u003c\/p\u003e \u003cp\u003e23.3.3.1 The Viral Glycan Shield 419\u003c\/p\u003e \u003cp\u003e23.3.3.2 Shed Viral Glycoproteins: An Antibody Decoy 421\u003c\/p\u003e \u003cp\u003e23.3.3.3 Antigenic Variations in Viral Glycoproteins 421\u003c\/p\u003e \u003cp\u003e23.3.3.4 Shed Viral Glycoproteins and Immune Signal Modulation 423\u003c\/p\u003e \u003cp\u003e23.3.4 Evading Host Restriction Factors 423\u003c\/p\u003e \u003cp\u003e23.3.5 Modulation of Other Immune Pathways 424\u003c\/p\u003e \u003cp\u003e23.4 Viral Entry Proteins Moonlighting as Saboteurs of Cellular Pathways 427\u003c\/p\u003e \u003cp\u003e23.4.1 Sabotaging Signal Transduction Cascades 427\u003c\/p\u003e \u003cp\u003e23.4.2 Host Surface Protein Sabotage 428\u003c\/p\u003e \u003cp\u003e23.5 Conclusions 429\u003c\/p\u003e \u003cp\u003eReferences 429\u003c\/p\u003e \u003cp\u003eIndex 439\u003c\/p\u003e","brand":"John Wiley and Sons Ltd","offers":[{"title":"Default Title","offer_id":49406954438999,"sku":"9781118951118","price":139.6,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781118951118.jpg?v=1730497679","url":"https:\/\/bookcurl.com\/products\/moonlighting-proteins-9781118951118","provider":"Book Curl","version":"1.0","type":"link"}