Moonlighting Proteins

1 - Title Page [Seite 5]
2 - Copyright Page [Seite 6]
3 - Contents [Seite 7]
4 - List of Contributors [Seite 17]
5 - Preface [Seite 21]
6 - About the Editor [Seite 25]
7 - Part I Overview of Protein Moonlighting [Seite 27]
7.1 - Chapter 1 What is Protein Moonlighting and Why is it Important? [Seite 29]
7.1.1 - 1.1 What is Protein Moonlighting? [Seite 29]
7.1.2 - 1.2 Why is Moonlighting Important? [Seite 31]
7.1.2.1 - 1.2.1 Many More Proteins Might Moonlight [Seite 31]
7.1.2.2 - 1.2.2 Protein Structure/Evolution [Seite 31]
7.1.2.3 - 1.2.3 Roles in Health and Disease [Seite 34]
7.1.2.3.1 - 1.2.3.1 Humans [Seite 34]
7.1.2.3.2 - 1.2.3.2 Bacteria [Seite 36]
7.1.3 - 1.3 Current questions [Seite 37]
7.1.3.1 - 1.3.1 How Many More Proteins Moonlight? [Seite 37]
7.1.3.2 - 1.3.2 How Can We Identify Additional Proteins That Moonlight and all the Moonlighting Functions of Proteins? [Seite 37]
7.1.3.3 - 1.3.3 In Developing Novel Therapeutics, How Can We Target the Appropriate Function of a Moonlighting Protein and Not Affect Other Functions of the Protein? [Seite 38]
7.1.3.4 - 1.3.4 How do Moonlighting Proteins get Targeted to More Than One Location in the Cell? [Seite 38]
7.1.3.5 - 1.3.5 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? [Seite 38]
7.1.4 - 1.4 Conclusions [Seite 39]
7.1.5 - References [Seite 39]
7.2 - Chapter 2 Exploring Structure-Function Relationships in Moonlighting Proteins [Seite 47]
7.2.1 - 2.1 Introduction [Seite 47]
7.2.2 - 2.2 Multiple Facets of Protein Function [Seite 48]
7.2.3 - 2.3 The Protein Structure-Function Paradigm [Seite 49]
7.2.4 - 2.4 Computational Approaches for Identifying Moonlighting Proteins [Seite 51]
7.2.5 - 2.5 Classification of Moonlighting Proteins [Seite 52]
7.2.5.1 - 2.5.1 Proteins with Distinct Sites for Different Functions in the Same Domain [Seite 53]
7.2.5.1.1 - 2.5.1.1 ?-Enolase, Streptococcus pneumonia [Seite 53]
7.2.5.1.2 - 2.5.1.2 Albaflavenone monooxygenase, Streptomyces coelicolor A3(2) [Seite 55]
7.2.5.1.3 - 2.5.1.3 MAPK1/ERK2, Homo sapiens [Seite 56]
7.2.5.2 - 2.5.2 Proteins with Distinct Sites for Different Functions in More Than One Domain [Seite 56]
7.2.5.2.1 - 2.5.2.1 Malate synthase, Mycobacterium tuberculosis [Seite 57]
7.2.5.2.2 - 2.5.2.2 BirA, Escherichia coli [Seite 57]
7.2.5.2.3 - 2.5.2.3 MRDI, Homo sapiens [Seite 59]
7.2.5.3 - 2.5.3 Proteins Using the Same Residues for Different Functions [Seite 59]
7.2.5.3.1 - 2.5.3.1 GAPDH E. coli [Seite 59]
7.2.5.3.2 - 2.5.3.2 Leukotriene A4 hydrolase, Homo sapiens [Seite 59]
7.2.5.4 - 2.5.4 Proteins Using Different Residues in the Same/Overlapping Site for Different Functions [Seite 60]
7.2.5.4.1 - 2.5.4.1 Phosphoglucose isomerase, Oryctolagus cuniculus, Mus musculus, Homo sapiens [Seite 60]
7.2.5.4.2 - 2.5.4.2 Aldolase, Plasmodium falciparum [Seite 62]
7.2.5.5 - 2.5.5 Proteins with Different Structural Conformations for Different Functions [Seite 62]
7.2.5.5.1 - 2.5.5.1 RfaH, E. coli [Seite 62]
7.2.6 - 2.6 Conclusions [Seite 63]
7.2.7 - References [Seite 65]
8 - Part II Proteins Moonlighting in Prokarya [Seite 71]
8.1 - Chapter 3 Overview of Protein Moonlighting in Bacterial Virulence [Seite 73]
8.1.1 - 3.1 Introduction [Seite 73]
8.1.2 - 3.2 The Meaning of Bacterial Virulence and Virulence Factors [Seite 73]
8.1.3 - 3.3 Affinity as a Measure of the Biological Importance of Proteins [Seite 75]
8.1.4 - 3.4 Moonlighting Bacterial Virulence Proteins [Seite 76]
8.1.4.1 - 3.4.1 Bacterial Proteins Moonlighting as Adhesins [Seite 78]
8.1.4.2 - 3.4.2 Bacterial Moonlighting Proteins That Act as Invasins [Seite 85]
8.1.4.3 - 3.4.3 Bacterial Moonlighting Proteins Involved in Nutrient Acquisition [Seite 85]
8.1.4.4 - 3.4.4 Bacterial Moonlighting Proteins Functioning as Evasins [Seite 86]
8.1.4.5 - 3.4.5 Bacterial Moonlighting Proteins with Toxin?like Actions [Seite 89]
8.1.5 - 3.5 Bacterial Moonlighting Proteins Conclusively Shown to be Virulence Factors [Seite 90]
8.1.6 - 3.6 Eukaryotic Moonlighting Proteins That Aid in Bacterial Virulence [Seite 92]
8.1.7 - 3.7 Conclusions [Seite 93]
8.1.8 - References [Seite 94]
8.2 - Chapter 4 Moonlighting Proteins as Cross-Reactive Auto-Antigens [Seite 107]
8.2.1 - 4.1 Autoimmunity and Conservation [Seite 107]
8.2.2 - 4.2 Immunogenicity of Conserved Proteins [Seite 108]
8.2.3 - 4.3 HSP Co-induction, Food, Microbiota, and T-cell Regulation [Seite 110]
8.2.3.1 - 4.3.1 HSP as Targets for T-Cell Regulation [Seite 111]
8.2.4 - 4.4 The Contribution of Moonlighting Virulence Factors to Immunological Tolerance [Seite 113]
8.2.5 - References [Seite 114]
9 - Part III Proteins Moonlighting in Bacterial Virulence [Seite 119]
10 - Part 3.1 Chaperonins: A Family of Proteins with Widespread Virulence Properties [Seite 121]
10.1 - Chapter 5 Chaperonin 60 Paralogs in Mycobacterium tuberculosis and Tubercle Formation [Seite 123]
10.1.1 - 5.1 Introduction [Seite 123]
10.1.2 - 5.2 Tuberculosis and the Tuberculoid Granuloma [Seite 123]
10.1.3 - 5.3 Mycobacterial Factors Responsible for Granuloma Formation [Seite 124]
10.1.4 - 5.4 Mycobacterium tuberculosis Chaperonin 60 Proteins, Macrophage Function, and Granuloma Formation [Seite 126]
10.1.4.1 - 5.4.1 Mycobacterium tuberculosis has Two Chaperonin 60 Proteins [Seite 126]
10.1.4.2 - 5.4.2 Moonlighting Actions of Mycobacterial Chaperonin 60 Proteins [Seite 127]
10.1.4.3 - 5.4.3 Actions of Mycobacterial Chaperonin 60 Proteins Compatible with the Pathology of Tuberculosis [Seite 128]
10.1.4.4 - 5.4.4 Identification of the Myeloid?Cell?Activating Site in M. tuberculosis Chaperonin 60.1 [Seite 131]
10.1.5 - 5.5 Conclusions [Seite 132]
10.1.6 - References [Seite 132]
10.2 - Chapter 6 Legionella pneumophila Chaperonin 60, an Extra- and Intra-Cellular Moonlighting Virulence-Related Factor [Seite 137]
10.2.1 - 6.1 Background [Seite 137]
10.2.2 - 6.2 HtpB is an Essential Chaperonin with Protein-folding Activity [Seite 138]
10.2.3 - 6.3 Experimental Approaches to Elucidate the Functional Mechanisms of HtpB [Seite 138]
10.2.3.1 - 6.3.1 The Intracellular Signaling Mechanism of HtpB in Yeast [Seite 139]
10.2.3.2 - 6.3.2 Yeast Two-Hybrid Screens [Seite 144]
10.2.4 - 6.4 Secretion Mechanisms Potentially Responsible for Transporting HtpB to Extracytoplasmic Locations [Seite 146]
10.2.4.1 - 6.4.1 Ability of GroEL and HtpB to Associate with Membranes [Seite 147]
10.2.4.2 - 6.4.2 Ongoing Mechanistic Investigations on Chaperonins Secretion [Seite 148]
10.2.5 - 6.5 Identifying Functionally Important Amino Acid Positions in HtpB [Seite 150]
10.2.5.1 - 6.5.1 Site-Directed Mutagenesis [Seite 151]
10.2.6 - 6.6 Functional Evolution of HtpB [Seite 152]
10.2.7 - 6.7 Concluding Remarks [Seite 153]
10.2.8 - References [Seite 155]
11 - Part 3.2 Peptidylprolyl Isomerases, Bacterial Virulence, and Targets for Therapy [Seite 161]
11.1 - Chapter 7 An Overview of Peptidylprolyl Isomerases (PPIs) in Bacterial Virulence [Seite 163]
11.1.1 - 7.1 Introduction [Seite 163]
11.1.2 - 7.2 Proline and PPIs [Seite 163]
11.1.3 - 7.3 Host PPIs and Responses to Bacteria and Bacterial Toxins [Seite 164]
11.1.4 - 7.4 Bacterial PPIs as Virulence Factors [Seite 164]
11.1.4.1 - 7.4.1 Proposed Mechanism of Virulence of Legionella pneumophila Mip [Seite 166]
11.1.5 - 7.5 Other Bacterial PPIs Involved in Virulence [Seite 166]
11.1.6 - 7.6 Conclusions [Seite 168]
11.1.7 - References [Seite 168]
12 - Part 3.3 Glyceraldehyde 3-Phosphate Dehydrogenase (GAPDH): A Multifunctional Virulence Factor [Seite 173]
12.1 - Chapter 8 GAPDH: A Multifunctional Moonlighting Protein in Eukaryotes and Prokaryotes [Seite 175]
12.1.1 - 8.1 Introduction [Seite 175]
12.1.2 - 8.2 GAPDH Membrane Function and Bacterial Virulence [Seite 176]
12.1.2.1 - 8.2.1 Bacterial GAPDH Virulence [Seite 177]
12.1.2.2 - 8.2.2 GAPDH and Iron Metabolism in Bacterial Virulence [Seite 179]
12.1.3 - 8.3 Role of Nitric Oxide in GAPDH Bacterial Virulence [Seite 179]
12.1.3.1 - 8.3.1 Nitric Oxide in Bacterial Virulence: Evasion of the Immune Response [Seite 180]
12.1.3.2 - 8.3.2 Formation of GAPDHcys-NO by Bacterial NO Synthases [Seite 181]
12.1.3.3 - 8.3.3 GAPDHcys-NO in Bacterial Virulence: Induction of Macrophage Apoptosis [Seite 181]
12.1.3.4 - 8.3.4 GAPDHcys-NO in Bacterial Virulence: Inhibition of Macrophage iNOS Activity [Seite 182]
12.1.3.5 - 8.3.5 GAPDHcys-NO in Bacterial Virulence: Transnitrosylation to Acceptor Proteins [Seite 183]
12.1.4 - 8.4 GAPDH Control of Gene Expression and Bacterial Virulence [Seite 184]
12.1.4.1 - 8.4.1 Bacterial GAPDH Virulence [Seite 185]
12.1.5 - 8.5 Discussion [Seite 186]
12.1.6 - Acknowledgements [Seite 188]
12.1.7 - References [Seite 188]
12.2 - Chapter 9 Streptococcus pyogenes GAPDH: A Cell-Surface Major Virulence Determinant [Seite 195]
12.2.1 - 9.1 Introduction and Early Discovery [Seite 195]
12.2.2 - 9.2 GAS GAPDH: A Major Surface Protein with Multiple Binding Activities [Seite 196]
12.2.3 - 9.3 AutoADP-Ribosylation of SDH and Other Post-Translational Modifications [Seite 198]
12.2.4 - 9.4 Implications of the Binding of SDH to Mammalian Proteins for Cell Signaling and Virulence Mechanisms [Seite 199]
12.2.5 - 9.5 Surface Export of SDH/GAPDH: A Cause or Effect? [Seite 204]
12.2.6 - 9.6 SDH: The GAS Virulence Factor-Regulating Virulence Factor [Seite 206]
12.2.7 - 9.7 Concluding Remarks and Future Perspectives [Seite 209]
12.2.8 - References [Seite 209]
12.3 - Chapter 10 Group B Streptococcus GAPDH and Immune Evasion [Seite 221]
12.3.1 - 10.1 The Bacterium GBS [Seite 221]
12.3.2 - 10.2 Neonates are More Susceptible to GBS Infection than Adults [Seite 221]
12.3.3 - 10.3 IL-10 Production Facilitates Bacterial Infection [Seite 222]
12.3.4 - 10.4 GBS Glyceraldehyde-3-Phosphate Dehydrogenase Induces IL-10 Production [Seite 223]
12.3.5 - 10.5 Summary [Seite 225]
12.3.6 - References [Seite 226]
12.4 - Chapter 11 Mycobacterium tuberculosis Cell-Surface GAPDH Functions as a Transferrin Receptor [Seite 231]
12.4.1 - 11.1 Introduction [Seite 231]
12.4.2 - 11.2 Iron Acquisition by Bacteria [Seite 232]
12.4.2.1 - 11.2.1 Heme Uptake [Seite 232]
12.4.2.2 - 11.2.2 Siderophore-Mediated Uptake [Seite 233]
12.4.2.3 - 11.2.3 Transferrin Iron Acquisition [Seite 233]
12.4.3 - 11.3 Iron Acquisition by Intracellular Pathogens [Seite 233]
12.4.4 - 11.4 Iron Acquisition by M. tb [Seite 234]
12.4.4.1 - 11.4.1 Heme Uptake [Seite 234]
12.4.4.2 - 11.4.2 Siderophore-Mediated Iron Acquisition [Seite 235]
12.4.4.3 - 11.4.3 Transferrin-Mediated Iron Acquisition [Seite 235]
12.4.5 - 11.5 Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) [Seite 236]
12.4.6 - 11.6 Macrophage GAPDH and Iron Uptake [Seite 236]
12.4.6.1 - 11.6.1 Regulation [Seite 236]
12.4.6.2 - 11.6.2 Mechanism of Iron Uptake and Efflux [Seite 237]
12.4.6.3 - 11.6.3 Role of Post-Translational Modifications [Seite 237]
12.4.7 - 11.7 Mycobacterial GAPDH and Iron Uptake [Seite 238]
12.4.7.1 - 11.7.1 Regulation [Seite 238]
12.4.7.2 - 11.7.2 Mechanism of Iron Uptake [Seite 241]
12.4.7.3 - 11.7.3 Uptake by Intraphagosomal M. tb [Seite 242]
12.4.8 - 11.8 Conclusions and Future Perspectives [Seite 242]
12.4.9 - Acknowledgements [Seite 244]
12.4.10 - References [Seite 245]
12.5 - Chapter 12 GAPDH and Probiotic Organisms [Seite 251]
12.5.1 - 12.1 Introduction [Seite 251]
12.5.2 - 12.2 Probiotics and Safety [Seite 251]
12.5.3 - 12.3 Potential Risk of Probiotics [Seite 253]
12.5.4 - 12.4 Plasminogen Binding and Enhancement of its Activation [Seite 254]
12.5.5 - 12.5 GAPDH as an Adhesin [Seite 255]
12.5.6 - 12.6 Binding Regions [Seite 258]
12.5.7 - 12.7 Mechanisms of Secretion and Surface Localization [Seite 260]
12.5.8 - 12.8 Other Functions [Seite 261]
12.5.9 - 12.9 Conclusion [Seite 262]
12.5.10 - References [Seite 263]
13 - Part 3.4 Cell-Surface Enolase: A Complex Virulence Factor [Seite 271]
13.1 - Chapter 13 Impact of Streptococcal Enolase in Virulence [Seite 273]
13.1.1 - 13.1 Introduction [Seite 273]
13.1.2 - 13.2 General Characteristics [Seite 274]
13.1.3 - 13.3 Expression and Surface Exposition of Enolase [Seite 275]
13.1.4 - 13.4 Streptococcal Enolase as Adhesion Cofactor [Seite 278]
13.1.4.1 - 13.4.1 Enolase as Plasminogen?Binding Protein [Seite 278]
13.1.4.1.1 - 13.4.1.1 Plasminogen-Binding Sites of Streptococcal Enolases [Seite 279]
13.1.4.2 - 13.4.2 Role of Enolase in Plasminogen-Mediated Bacterial-Host Cell Adhesion and Internalization [Seite 280]
13.1.4.3 - 13.4.3 Enolase as Plasminogen-Binding Protein in Non-Pathogenic Bacteria [Seite 281]
13.1.5 - 13.5 Enolase as Pro-Fibrinolytic Cofactor [Seite 282]
13.1.5.1 - 13.5.1 Degradation of Fibrin Thrombi and Components of the Extracellular Matrix [Seite 283]
13.1.6 - 13.6 Streptococcal Enolase as Cariogenic Factor in Dental Disease [Seite 284]
13.1.7 - 13.7 Conclusion [Seite 284]
13.1.8 - Acknowledgement [Seite 285]
13.1.9 - References [Seite 285]
13.2 - Chapter 14 Streptococcal Enolase and Immune Evasion [Seite 295]
13.2.1 - 14.1 Introduction [Seite 295]
13.2.2 - 14.2 Localization and Crystal Structure [Seite 297]
13.2.3 - 14.3 Multiple Binding Activities of ?-Enolase [Seite 299]
13.2.4 - 14.4 Involvement of ?-Enolase in Gene Expression Regulation [Seite 302]
13.2.5 - 14.5 Role of Anti-?-Enolase Antibodies in Host Immunity [Seite 303]
13.2.6 - 14.6 ?-Enolase as Potential Therapeutic Target [Seite 305]
13.2.7 - 14.7 Questions Concerning ?-Enolase [Seite 307]
13.2.8 - References [Seite 307]
13.3 - Chapter 15 Borrelia burgdorferi Enolase and Plasminogen Binding [Seite 317]
13.3.1 - 15.1 Introduction to Lyme Disease [Seite 317]
13.3.2 - 15.2 Life Cycle [Seite 318]
13.3.3 - 15.3 Borrelia Virulence Factors [Seite 318]
13.3.4 - 15.4 Plasminogen Binding by Bacteria [Seite 319]
13.3.5 - 15.5 B. burgdorferi and Plasminogen Binding [Seite 320]
13.3.6 - 15.6 Enolase [Seite 321]
13.3.7 - 15.7 B. burgdorferi Enolase and Plasminogen Binding [Seite 323]
13.3.8 - 15.8 Concluding Thoughts [Seite 327]
13.3.9 - Acknowledgements [Seite 327]
13.3.10 - References [Seite 327]
14 - Part 3.5 Other Glycolytic Enzymes Acting as Virulence Factors [Seite 335]
14.1 - Chapter 16 Triosephosphate Isomerase from?Staphylococcus aureus and Plasminogen Receptors on Microbial Pathogens [Seite 337]
14.1.1 - 16.1 Introduction [Seite 337]
14.1.2 - 16.2 Identification of Triosephosphate Isomerase on S. aureus as a Molecule that Binds to the Pathogenic Yeast C. neoformans [Seite 338]
14.1.2.1 - 16.2.1 Co-Cultivation of S. aureus and C. neoformans [Seite 338]
14.1.2.2 - 16.2.2 Identification of Adhesins on S. aureus and C. neoformans [Seite 338]
14.1.2.3 - 16.2.3 Mechanisms of C. neoformans Cell Death [Seite 339]
14.1.3 - 16.3 Binding of Triosephosphate Isomerase with Human Plasminogen [Seite 340]
14.1.4 - 16.4 Plasminogen-Binding Proteins on Trichosporon asahii [Seite 340]
14.1.5 - 16.5 Plasminogen Receptors on C. neoformans [Seite 342]
14.1.6 - 16.6 Conclusions [Seite 342]
14.1.7 - References [Seite 343]
14.2 - Chapter 17 Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases [Seite 347]
14.2.1 - 17.1 Introduction [Seite 347]
14.2.2 - 17.2 Fructose 1,6-bisphosphate Aldolase in Metabolism [Seite 347]
14.2.3 - 17.3 Surface Localization of Streptococcal Fructose 1,6-bisphosphate Aldolases [Seite 348]
14.2.4 - 17.4 Pneumococcal FBA Adhesin Binds Flamingo Cadherin Receptor [Seite 349]
14.2.5 - 17.5 FBA is Required for Optimal Meningococcal Adhesion to Human Cells [Seite 350]
14.2.6 - 17.6 Mycobacterium tuberculosis FBA Binds Human Plasminogen [Seite 351]
14.2.7 - 17.7 Other Examples of FBAs with Possible Roles in Pathogenesis [Seite 352]
14.2.8 - 17.8 Conclusions [Seite 353]
14.2.9 - References [Seite 353]
15 - Part 3.6 Other Metabolic Enzymes Functioning in Bacterial Virulence [Seite 359]
15.1 - Chapter 18 Pyruvate Dehydrogenase Subunit B and Plasminogen Binding in Mycoplasma [Seite 361]
15.1.1 - 18.1 Introduction [Seite 361]
15.1.2 - 18.2 Binding of Human Plasminogen to M. pneumoniae [Seite 363]
15.1.3 - 18.3 Localization of PDHB on the Surface of M. pneumoniae Cells [Seite 366]
15.1.4 - 18.4 Conclusions [Seite 369]
15.1.5 - References [Seite 370]
16 - Part 3.7 Miscellaneous Bacterial Moonlighting Virulence Proteins [Seite 375]
16.1 - Chapter 19 Unexpected Interactions of Leptospiral Ef-Tu and Enolase [Seite 377]
16.1.1 - 19.1 Leptospira -Host Interactions [Seite 377]
16.1.2 - 19.2 Leptospira Ef-Tu [Seite 378]
16.1.3 - 19.3 Leptospira Enolase [Seite 379]
16.1.4 - 19.4 Conclusions [Seite 380]
16.1.5 - References [Seite 380]
16.2 - Chapter 20 Mycobacterium tuberculosis Antigen 85 Family Proteins: Mycolyl Transferases and Matrix-Binding Adhesins [Seite 383]
16.2.1 - 20.1 Introduction [Seite 383]
16.2.2 - 20.2 Identification of Antigen 85 [Seite 384]
16.2.3 - 20.3 Antigen 85 Family Proteins: Mycolyl Transferases [Seite 385]
16.2.3.1 - 20.3.1 Role of the Mycomembrane [Seite 385]
16.2.3.2 - 20.3.2 Ag85 Family of Homologous Proteins [Seite 385]
16.2.3.3 - 20.3.3 Inhibition and Knockouts of Ag85 [Seite 386]
16.2.4 - 20.4 Antigen 85 Family Proteins: Matrix-Binding Adhesins [Seite 387]
16.2.4.1 - 20.4.1 Abundance and Location [Seite 387]
16.2.4.2 - 20.4.2 Ag85 a Fibronectin-Binding Adhesin [Seite 388]
16.2.4.3 - 20.4.3 Ag85 an Elastin-Binding Adhesin [Seite 389]
16.2.4.4 - 20.4.4 Implication in Disease [Seite 390]
16.2.5 - 20.5 Conclusion [Seite 391]
16.2.6 - Acknowledgement [Seite 391]
16.2.7 - References [Seite 391]
17 - Part 3.8 Bacterial Moonlighting Proteins that Function as Cytokine Binders/Receptors [Seite 397]
17.1 - Chapter 21 Miscellaneous IL-1?-Binding Proteins of Aggregatibacter actinomycetemcomitans [Seite 399]
17.1.1 - 21.1 Introduction [Seite 399]
17.1.2 - 21.2 A. actinomycetemcomitans Biofilms Sequester IL-1? [Seite 400]
17.1.3 - 21.3 A. actinomycetemcomitans Cells Take in IL-1? [Seite 401]
17.1.3.1 - 21.3.1 Novel Outer Membrane Lipoprotein of ?A. actinomycetemcomitans Binds IL-1? [Seite 401]
17.1.3.2 - 21.3.2 IL-1? Localizes to the Cytosolic Face of the Inner Membrane and in the Nucleoids of ?A. actinomycetemcomitans [Seite 403]
17.1.3.3 - 21.3.3 Inner Membrane Protein ATP Synthase Subunit ? Binds IL-1? [Seite 403]
17.1.3.4 - 21.3.4 DNA-Binding Histone-Like Protein HU Interacts with IL-1? [Seite 404]
17.1.4 - 21.4 The Potential Effects of IL-1? on A. actinomycetemcomitans [Seite 405]
17.1.4.1 - 21.4.1 Biofilm Amount Increases and Metabolic Activity Decreases [Seite 405]
17.1.4.2 - 21.4.2 Potential Changes in Gene Expression [Seite 406]
17.1.5 - 21.5 Conclusions [Seite 407]
17.1.6 - References [Seite 408]
18 - Part 3.9 Moonlighting Outside of the Box [Seite 413]
18.1 - Chapter 22 Bacteriophage Moonlighting Proteins in the Control of Bacterial Pathogenicity [Seite 415]
18.1.1 - 22.1 Introduction [Seite 415]
18.1.2 - 22.2 Bacteriophage T4 I-TevI Homing Endonuclease Functions as a Transcriptional Autorepressor [Seite 417]
18.1.3 - 22.3 Capsid Psu Protein of Bacteriophage P4 Functions as a Rho Transcription Antiterminator [Seite 420]
18.1.4 - 22.4 Bacteriophage Lytic Enzymes Moonlight as Structural Proteins [Seite 424]
18.1.5 - 22.5 Moonlighting Bacteriophage Proteins De-Repressing Phage-Inducible Chromosomal Islands [Seite 424]
18.1.6 - 22.6 dUTPase, a Metabolic Enzyme with a Moonlighting Signalling Role [Seite 427]
18.1.7 - 22.7 Escherichia coli Thioredoxin Protein Moonlights with T7 DNA Polymerase for Enhanced T7 DNA Replication [Seite 430]
18.1.8 - 22.8 Discussion [Seite 430]
18.1.9 - References [Seite 432]
18.2 - Chapter 23 Viral Entry Glycoproteins and Viral Immune Evasion [Seite 439]
18.2.1 - 23.1 Introduction [Seite 439]
18.2.2 - 23.2 Enveloped Viral Entry [Seite 440]
18.2.3 - 23.3 Moonlighting Activities of Viral Entry Glycoproteins [Seite 441]
18.2.3.1 - 23.3.1 Viral Entry Glycoproteins Moonlighting as Evasins [Seite 442]
18.2.3.2 - 23.3.2 Evading the Complement System [Seite 443]
18.2.3.3 - 23.3.3 Evading Antibody Surveillance [Seite 445]
18.2.3.3.1 - 23.3.3.1 The Viral Glycan Shield [Seite 445]
18.2.3.3.2 - 23.3.3.2 Shed Viral Glycoproteins: An Antibody Decoy [Seite 447]
18.2.3.3.3 - 23.3.3.3 Antigenic Variations in Viral Glycoproteins [Seite 447]
18.2.3.3.4 - 23.3.3.4 Shed Viral Glycoproteins and Immune Signal Modulation [Seite 449]
18.2.3.4 - 23.3.4 Evading Host Restriction Factors [Seite 449]
18.2.3.5 - 23.3.5 Modulation of Other Immune Pathways [Seite 450]
18.2.4 - 23.4 Viral Entry Proteins Moonlighting as Saboteurs of Cellular Pathways [Seite 453]
18.2.4.1 - 23.4.1 Sabotaging Signal Transduction Cascades [Seite 453]
18.2.4.2 - 23.4.2 Host Surface Protein Sabotage [Seite 454]
18.2.5 - 23.5 Conclusions [Seite 455]
18.2.6 - References [Seite 455]
19 - Index [Seite 465]
20 - Supplemental Images [Seite 480]
21 - EULA [Seite 496]