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Moonlighting proteins : novel virulence factors in bacterial infections

PrefaceI Overview of Protein Moonlighting What is Protein Moonlighting and Why is it Important?What is Protein Moonlighting?Why is Moonlighting Important?Many More Proteins Might MoonlightProtein Structure/EvolutionRoles in Health and DiseaseHumansBacteriaCurrent questionsHow Many More Proteins Moonlight?How Can We Identify Additional Proteins That Moonlight and all the Moonlighting Functions of Proteins?In Developing Novel Therapeutics, How Can We Target the Appropriate Function of a Moonlighting Protein and Not Affect Other Functions of the Protein?How do Moonlighting Proteins get Targeted to More Than One Location in the Cell?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?ConclusionsReferencesExploring Structure-Function Relationships in Moonlighting ProteinsIntroductionMultiple Facets of Protein FunctionThe Protein Structure-Function ParadigmComputational Approaches for Identifying Moonlighting ProteinsClassification of Moonlighting ProteinsProteins with Distinct Sites for Different Functions in the Same Domaina-Enolase, Streptococcus pneumoniaAlbaflavenone monooxygenase, Streptomyces coelicolor A3(2)MAPK1/ERK2, Homo sapiensProteins with Distinct Sites for Different Functions in More Than One DomainMalate synthase, Mycobacterium tuberculosisBir A, Escherichia coliMRDI, Homo sapiensProteins Using the Same Residues for Different FunctionsGAPDH E. coliLeukotriene A4 hydrolase, Homo sapiensProteins Using Different Residues in the Same/Overlapping Site for Different FunctionsPhosphoglucose isomerase, Oryctolagus cuniculus, Mus musculus, Homo sapiensAldolase, Plasmodium falciparumProteins with Different Structural Conformations for Different FunctionsRfaH, E. coliConclusionsReferencesII Proteins Moonlighting in ProkaryaOverview of Protein Moonlighting in Bacterial VirulenceIntroductionThe Meaning of Bacterial Virulence and Virulence FactorsAffinity as a Measure of the Biological Importance of ProteinsMoonlighting Bacterial Virulence ProteinsBacterial Proteins Moonlighting as AdhesinsBacterial Moonlighting Proteins That Act as InvasinsBacterial Moonlighting Proteins Involved in Nutrient AcquisitionBacterial Moonlighting Proteins Functioning as EvasinsBacterial Moonlighting Proteins with Toxin-like ActionsBacterial Moonlighting Proteins Conclusively Shown to be Virulence FactorsEukaryotic Moonlighting Proteins That Aid in Bacterial VirulenceConclusionsReferencesMoonlighting Proteins as Cross-Reactive Auto-AntigensAutoimmunity and ConservationImmunogenicity of Conserved ProteinsHSP Co-induction, Food, Microbiota, and T-cell RegulationHSP as Targets for T-Cell RegulationThe Contribution of Moonlighting Virulence Factors to Immunological ToleranceReferencesIII Proteins Moonlighting in Bacterial Virulence Chaperonins: A Family of Proteins with Widespread Virulence Properties Chaperonin 60 Paralogs in Mycobacterium tuberculosis and Tubercle FormationIntroductionTuberculosis and the Tuberculoid GranulomaMycobacterial Factors Responsible for Granuloma FormationMycobacterium tuberculosis Chaperonin 60 Proteins, Macrophage Function, and Granuloma FormationMycobacterium tuberculosis has Two Chaperonin 60 ProteinsMoonlighting Actions of Mycobacterial Chaperonin 60 ProteinsActions of Mycobacterial Chaperonin 60 Proteins Compatible with the Pathology of TuberculosisIdentification of the Myeloid-Cell-Activating Site in M. tuberculosis Chaperonin 60.1ConclusionsReferencesLegionella pneumophila Chaperonin 60, an Extra- and Intra-Cellular Moonlighting Virulence-Related FactorBackgroundHtpB is an Essential Chaperonin with Protein-folding ActivityExperimental Approaches to Elucidate the Functional Mechanisms of HtpBThe Intracellular Signaling Mechanism of HtpB in YeastYeast Two-Hybrid ScreensSecretion Mechanisms Potentially Responsible for Transporting HtpB to Extracytoplasmic LocationsAbility of GroEL and HtpB to Associate with MembranesOngoing Mechanistic Investigations on Chaperonins SecretionIdentifying Functionally Important Amino Acid Positions in HtpBSite-Directed MutagenesisFunctional Evolution of HtpBConcluding RemarksReferencesPeptidylprolyl Isomerases, Bacterial Virulence, and Targets for TherapyAn Overview of Peptidylprolyl Isomerases (PPIs) in Bacterial VirulenceIntroductionProline and PPIsHost PPIs and Responses to Bacteria and Bacterial ToxinsBacterial PPIs as Virulence FactorsProposed Mechanism of Virulence of Legionella pneumophila MipOther Bacterial PPIs Involved in VirulenceConclusionsReferencesGlyceraldehyde 3-Phosphate Dehydrogenase (GAPDH): A Multifunctional Virulence Factor GAPDH: A Multifunctional Moonlighting Protein in Eukaryotes and ProkaryotesIntroductionGAPDH Membrane Function and Bacterial VirulenceBacterial GAPDH VirulenceGAPDH and Iron Metabolism in Bacterial VirulenceRole of Nitric Oxide in GAPDH Bacterial VirulenceNitric Oxide in Bacterial Virulence: Evasion of the Immune ResponseFormation of GAPDHcys'NO by Bacterial NO SynthasesGAPDHcysNO in Bacterial Virulence: Induction of Macrophage ApoptosisGAPDHcysNO in Bacterial Virulence: Inhibition of Macrophage iNOS ActivityGAPDHcysNO in Bacterial Virulence: Transnitrosylation to Acceptor ProteinsGAPDH Control of Gene Expression and Bacterial VirulenceBacterial GAPDH VirulenceDiscussionAcknowledgementsReferencesStreptococcus pyogenes GAPDH: A Cell-Surface Major Virulence DeterminantIntroduction and Early DiscoveryGAS GAPDH: A Major Surface Protein with Multiple Binding ActivitiesAutoADP-Ribosylation of SDH and Other Post-Translational ModificationsImplications of the Binding of SDH to Mammalian Proteins for Cell Signaling and Virulence MechanismsSurface Export of SDH/GAPDH: A Cause or Effect?SDH: The GAS Virulence Factor-Regulating Virulence FactorConcluding Remarks and Future PerspectivesReferencesGroup B Streptococcus GAPDH and Immune EvasionThe Bacterium GBSNeonates are More Susceptible to GBS Infection than AdultsIL-10 Production Facilitates Bacterial InfectionGBS Glyceraldehyde-3-Phosphate Dehydrogenase Induces IL-10 ProductionSummaryReferencesMycobacterium tuberculosis Cell-Surface GAPDH Functions as a Transferrin ReceptorIntroductionIron Acquisition by BacteriaHeme UptakeSiderophore-Mediated UptakeTransferrin Iron AcquisitionIron Acquisition by Intracellular PathogensIron Acquisition by M. tbHeme UptakeSiderophore-Mediated Iron AcquisitionTransferrin-Mediated Iron AcquisitionGlyceraldehyde-3-Phosphate Dehydrogenase (GAPDH)Macrophage GAPDH and Iron UptakeRegulationMechanism of Iron Uptake and EffluxRole of Post-Translational ModificationsMycobacterial GAPDH and Iron UptakeRegulationMechanism of Iron UptakeUptake by Intraphagosomal M. tbConclusions and Future PerspectivesAcknowledgementsReferencesGAPDH and Probiotic OrganismsIntroductionProbiotics and SafetyPotential Risk of ProbioticsPlasminogen Binding and Enhancement of its ActivationGAPDH as an AdhesinBinding RegionsMechanisms of Secretion and Surface LocalizationOther FunctionsConclusionReferencesCell-Surface Enolase: A Complex Virulence FactorImpact of Streptococcal Enolase in VirulenceIntroductionGeneral CharacteristicsExpression and Surface Exposition of EnolaseStreptococcal Enolase as Adhesion CofactorEnolase as Plasminogen-Binding ProteinRole of Enolase in Plasminogen-Mediated Bacterial-Host Cell Adhesion and InternalizationEnolase as Plasminogen-Binding Protein in Non-Pathogenic BacteriaEnolase as Pro-Fibrinolytic CofactorDegradation of Fibrin Thrombi and Components of the Extracellular MatrixStreptococcal Enolase as Cariogenic Factor in Dental DiseaseConclusionAcknowledgementReferencesStreptococcal Enolase and Immune EvasionIntroductionLocalization and Crystal StructureMultiple Binding Activities of a-EnolaseInvolvement of a-Enolase in Gene Expression RegulationRole of Anti-a-Enolase Antibodies in Host Immunitya-Enolase as Potential Therapeutic TargetQuestions Concerning a-EnolaseReferencesBorrelia burgdorferi Enolase and Plasminogen BindingIntroduction to Lyme DiseaseLife CycleBorrelia Virulence FactorsPlasminogen Binding by BacteriaB. burgdorferi and Plasminogen BindingEnolaseB. burgdorferi Enolase and Plasminogen BindingConcluding ThoughtsAcknowledgementsReferencesOther Glycolytic Enzymes Acting as Virulence FactorsTriosephosphate Isomerase from Staphylococcus aureus and Plasminogen Receptors on Microbial PathogensIntroductionIdentification of Triosephosphate Isomerase on S. aureus as a Molecule that Binds to the Pathogenic Yeast C. neoformansCo-Cultivation of S. aureus and C. neoformansIdentification of Adhesins on S. aureus and C. neoformansMechanisms of C. neoformans Cell DeathBinding of Triosephosphate Isomerase with Human PlasminogenPlasminogen-Binding Proteins on Trichosporon asahiiPlasminogen Receptors on C. neoformansConclusionsReferencesMoonlighting Functions of Bacterial Fructose 1,6-Bisphosphate AldolasesIntroductionFructose 1,6-bisphosphate Aldolase in MetabolismSurface Localization of Streptococcal Fructose 1,6-bisphosphate AldolasesPneumococcal FBA Adhesin Binds Flamingo Cadherin ReceptorFBA is Required for Optimal Meningococcal Adhesion to Human CellsMycobacterium tuberculosis FBA Binds Human PlasminogenOther Examples of FBAs with Possible Roles in PathogenesisConclusionsReferencesOther Metabolic Enzymes Functioning in Bacterial Virulence Pyruvate Dehydrogenase Subunit B and Plasminogen Binding in MycoplasmaIntroductionBinding of Human Plasminogen to M. pneumoniaeLocalization of PDHB on the Surface of M. pneumoniae CellsConclusionsReferencesMiscellaneous Bacterial Moonlighting Virulence Proteins Unexpected Interactions of Leptospiral Ef-Tu and EnolaseLeptospira -Host InteractionsLeptospira Ef-TuLeptospira EnolaseConclusionsReferencesMycobacterium tuberculosis Antigen 85 Family Proteins: Mycolyl Transferases and Matrix-Binding AdhesinsIntroductionIdentification of Antigen 85Antigen 85 Family Proteins: Mycolyl TransferasesRole of the MycomembraneAg85 Family of Homologous ProteinsInhibition and Knockouts of Ag85Antigen 85 Family Proteins: Matrix-Binding AdhesinsAbundance and LocationAg85 a Fibronectin-Binding AdhesinAg85 an Elastin-Binding AdhesinImplication in DiseaseConclusionAcknowledgementReferencesBacterial Moonlighting Proteins that Function as Cytokine Binders/ReceptorsMiscellaneous IL-10-Binding Proteins of Aggregatibacter actinomycetemcomitansIntroductionA. actinomycetemcomitans Biofilms Sequester IL-ipA. actinomycetemcomitans Cells Take in IL-1 вNovel Outer Membrane Lipoprotein of A. actinomycetemcomitans Binds IL-1 вIL-1 в Localizes to the Cytosolic Face of the Inner Membrane and in the Nucleoids of A. actinomycetemcomitansInner Membrane Protein ATP Synthase Subunit в Binds IL-1 вDNA-Binding Histone-Like Protein HU Interacts with IL-1 вThe Potential Effects of IL-1 в on A. actinomycetemcomitansBiofilm Amount Increases and Metabolic Activity DecreasesPotential Changes in Gene ExpressionConclusionsReferencesMoonlighting Outside of the BoxBacteriophage Moonlighting Proteins in the Control of Bacterial PathogenicityIntroductionBacteriophage T4 I-TevI Homing Endonuclease Functions as a Transcriptional AutorepressorCapsid Psu Protein of Bacteriophage P4 Functions as a Rho Transcription AntiterminatorBacteriophage Lytic Enzymes Moonlight as Structural ProteinsMoonlighting Bacteriophage Proteins De-Repressing Phage-Inducible Chromosomal IslandsdUTPase, a Metabolic Enzyme with a Moonlighting Signalling RoleEscherichia coli Thioredoxin Protein Moonlights with T7 DNA Polymerase for Enhanced T7 DNA ReplicationDiscussionReferencesViral Entry Glycoproteins and Viral Immune EvasionIntroductionEnveloped Viral EntryMoonlighting Activities of Viral Entry GlycoproteinsViral Entry Glycoproteins Moonlighting as EvasinsEvading the Complement SystemEvading Antibody SurveillanceEvading Host Restriction FactorsModulation of Other Immune PathwaysViral Entry Proteins Moonlighting as Saboteurs of Cellular PathwaysSabotaging Signal Transduction CascadesHost Surface Protein SabotageConclusionsReferences
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