2001
Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells
Murli S, Watson R, Galán J. Role of tyrosine kinases and the tyrosine phosphatase SptP in the interaction of Salmonella with host cells. Cellular Microbiology 2001, 3: 795-810. PMID: 11736992, DOI: 10.1046/j.1462-5822.2001.00158.x.Peer-Reviewed Original ResearchMeSH KeywordsActinsBacterial ProteinsCdc42 GTP-Binding ProteinCell NucleusCytoskeletonInterleukin-8Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPhosphorylationPhosphotyrosineProtein Tyrosine PhosphatasesProtein-Tyrosine KinasesSalmonellaSalmonella typhimuriumSignal TransductionSubstrate SpecificityTransfectionTyrosineVimentinConceptsTyrosine phosphatase activityBacterial proteinsCellular responsesPhosphatase activityTyrosine kinaseHost cellsType III secretion systemIntermediate filament protein vimentinCarboxy-terminal domainRho family GTPases Cdc42Actin cytoskeleton reorganizationCellular transcription factorsMAP kinase activationInteraction of SalmonellaMembrane rufflesGAP activitySpecialized organellesGTPases Cdc42Secretion systemTranscription factorsCytoskeleton reorganizationKinase activationProtein vimentinBacterial uptakeProteinMaintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
Stebbins C, Galán J. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 2001, 414: 77-81. PMID: 11689946, DOI: 10.1038/35102073.Peer-Reviewed Original ResearchConceptsEffector proteinsSecretion systemType III protein secretion systemBacterial type III secretionSpecific cytosolic chaperonesSuch effector proteinsType III secretion systemSecretion-competent stateVirulence effector proteinsProtein secretion systemChaperone-binding domainHost cell cytosolType III secretionType III apparatusCytosolic chaperonesUnfolded polypeptidesSecretion machineryCognate chaperoneÅ resolutionChaperonesCell cytosolChaperone moleculesEffective translocationBacterial pathogensHydrophobic interfaceStructural mimicry in bacterial virulence
Stebbins C, Galán J. Structural mimicry in bacterial virulence. Nature 2001, 412: 701-705. PMID: 11507631, DOI: 10.1038/35089000.Peer-Reviewed Original ResearchConceptsAmino acid sequence similarityConvergent evolutionCellular functionsSequence similarityDirect homologuesBacterial virulenceHost proteinsNew effectorsMicrobial pathogensFunctional mimicryStructural mimicryMolecular levelVirulence factorsMimicryStructural studiesHost factorsImportant mechanismHost activityHomologuesVirulenceEffectorsProteinPathogensSimilarity
2000
Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1
Stebbins C, Galán J. Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1. Molecular Cell 2000, 6: 1449-1460. PMID: 11163217, DOI: 10.1016/s1097-2765(00)00141-6.Peer-Reviewed Original ResearchMeSH KeywordsAluminum CompoundsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding SitesCdc42 GTP-Binding ProteinCrystallography, X-RayDimerizationEvolution, MolecularFluoridesGTPase-Activating ProteinsGuanosine DiphosphateMacromolecular SubstancesModels, MolecularMolecular Sequence DataMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein Tyrosine PhosphatasesRac1 GTP-Binding ProteinRecombinant Fusion ProteinsSalmonella typhimuriumSequence AlignmentSignal Transduction
1999
A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
Fu Y, Galán J. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 1999, 401: 293-297. PMID: 10499590, DOI: 10.1038/45829.Peer-Reviewed Original ResearchMeSH KeywordsActinsArginineBacterial AdhesionBacterial ProteinsCdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsCell MembraneEscherichia coliGTPase-Activating ProteinsGTP-Binding ProteinsHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesMutationProtein KinasesProtein Tyrosine PhosphatasesProteinsRecombinant Fusion ProteinsSalmonella typhimuriumConceptsHost cell cytosolActin cytoskeletonType III secretion systemProtein secretion systemSpecialized protein secretion systemActin cytoskeleton reorganizationCell actin cytoskeletonActin cytoskeletal changesRho GTPase proteinsRac-1Bacterial effectorsEffector proteinsExchange factorGTPase proteinsSecretion systemSalmonella proteinsCytoskeletal changesCellular responsesCdc42ProteinInfected cellsBacterial invasionCytosolBacteriumSPTP
1998
Delivery of Epitopes by the Salmonella Type III Secretion System for Vaccine Development
Rüssmann H, Shams H, Poblete F, Fu Y, Galán J, Donis R. Delivery of Epitopes by the Salmonella Type III Secretion System for Vaccine Development. Science 1998, 281: 565-568. PMID: 9677200, DOI: 10.1126/science.281.5376.565.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationAntigens, ViralBacterial ProteinsCytosolEndoplasmic ReticulumEpitopesHistocompatibility Antigens Class IHybridomasLymphocytic ChoriomeningitisLymphocytic choriomeningitis virusMiceMice, Inbred C57BLNucleoproteinsPeptide FragmentsProtein Tyrosine PhosphatasesRecombinant Fusion ProteinsSalmonella typhimuriumT-LymphocytesT-Lymphocytes, CytotoxicTumor Cells, CulturedVaccines, SyntheticViral Core ProteinsViral VaccinesConceptsImmune responseClass IS. typhimuriumAntigen delivery systemAntigen delivery vectorDelivery of epitopesSalmonella type III secretion systemLethal infectionViral epitopesVaccine developmentHost cell cytosolType III secretion systemInfectionSecretion systemIntracellular stagesAvirulent strainsEpitopesEfficient inducerSalmonella typhimuriumTyphimuriumDelivery systemResponseType III protein secretion systemIdentification of a Specific Chaperone for SptP, a Substrate of the Centisome 63 Type III Secretion System ofSalmonella typhimurium
Fu Y, Galán J. Identification of a Specific Chaperone for SptP, a Substrate of the Centisome 63 Type III Secretion System ofSalmonella typhimurium. Journal Of Bacteriology 1998, 180: 3393-3399. PMID: 9642193, PMCID: PMC107295, DOI: 10.1128/jb.180.13.3393-3399.1998.Peer-Reviewed Original ResearchMeSH KeywordsActinsAmino Acid SequenceBacterial ProteinsBase SequenceChromosomes, BacterialCloning, MolecularComplement Inactivator ProteinsCytoskeletonKineticsMolecular Sequence DataPlasmidsPolymerase Chain ReactionProtein Tyrosine PhosphatasesRecombinant Fusion ProteinsSalmonella typhimuriumSequence AlignmentSequence Homology, Amino AcidConceptsType III secretion systemSecretion systemSpecific chaperonesActin cytoskeletonTyrosine phosphataseType III protein secretion systemHost cell actin cytoskeletonHost cellsProtein secretion systemCell actin cytoskeletonHost cell responsesPulse-chase experimentsCytoplasmic chaperonesCentisome 63Effector proteinsTranscription factorsAcidic polypeptidesChaperonesResidues 15Function mutationsEffector moleculesCytoskeletonProteinSPTPSalmonella typhimuriumThe Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton
Fu Y, Galán J. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Molecular Microbiology 1998, 27: 359-368. PMID: 9484891, DOI: 10.1046/j.1365-2958.1998.00684.x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAntigens, BacterialBacterial ProteinsCell LineCytoskeletonEpithelial CellsMembrane ProteinsProtein Tyrosine PhosphatasesRecombinant Fusion ProteinsSalmonella typhimuriumConceptsActin cytoskeletonHost cell actin cytoskeletonFusion proteinHost cellsAmino acidsAmino-terminal halfCell actin cytoskeletonCultured cells resultsWild-type toxinCultured epithelial cellsEffector proteinsModular domainsStress fibersActive GSTCytoskeletonProteinCells resultsEpithelial cellsGSTSPTPProlonged incubationTranslocationCellsS. typhimuriumMicroinjection
1996
A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurlum
Kaniga K, Uralil J, Bliska J, Galán J. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurlum. Molecular Microbiology 1996, 21: 633-641. PMID: 8866485, DOI: 10.1111/j.1365-2958.1996.tb02571.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBase SequenceCell LineChromosomes, BacterialDisease Models, AnimalDNA, BacterialEpithelial CellsFemaleHumansMacrophagesMiceMice, Inbred BALB CMolecular Sequence DataProtein Tyrosine PhosphatasesSalmonella InfectionsSalmonella typhimuriumSequence Homology, Amino AcidVirulenceConceptsProtein tyrosine phosphataseTyrosine phosphataseEffector proteinsCatalytic domainHost cell signal transduction pathwaysBacterial pathogen Salmonella typhimuriumSignal transduction pathwaysCritical Cys residuesAmino-terminal regionCarboxy-terminal regionPathogen Salmonella typhimuriumCell regulatory moleculesSequence similarityEffector domainSignaling functionsExport proteinCys residuesRegulatory moleculesExoenzyme SSequence analysisPeptide substratesPhosphatase activityCatalytic mechanismProteinYersinia spp