2022
Assembly and architecture of the type III secretion sorting platform
Soto J, Galán J, Lara-Tejero M. Assembly and architecture of the type III secretion sorting platform. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2218010119. PMID: 36512499, PMCID: PMC9907115, DOI: 10.1073/pnas.2218010119.Peer-Reviewed Original ResearchConceptsType III secretion machinesType III secretion systemTarget eukaryotic cellsType III secretionSecretion of proteinsBacterial nanomachinesSecretion machineEukaryotic cellsExport pathwayImportant bacterial pathogensSecretion systemBacterial structureAntivirulence strategiesCoordinated mechanismFunctional complexityBacterial pathogensGenetic deletionStructure modelingProtein deliveryAssemblyRational developmentCross-linking strategyAssembly processProteinDeletion
2006
Differential activation and function of Rho GTPases during Salmonella–host cell interactions
Patel JC, Galán J. Differential activation and function of Rho GTPases during Salmonella–host cell interactions. Journal Of Cell Biology 2006, 175: 453-463. PMID: 17074883, PMCID: PMC2064522, DOI: 10.1083/jcb.200605144.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBacterial Proteinscdc42 GTP-Binding ProteinCell MembraneChlorocebus aethiopsCOS CellsEnzyme ActivationGuanine Nucleotide Exchange FactorsHumansIntestinal MucosaMutationrac1 GTP-Binding Proteinrho GTP-Binding ProteinsRNA InterferenceSalmonella InfectionsSalmonella typhimuriumTransfectionConceptsRho family GTPasesExchange factorCellular responsesRho family guanosine triphosphatasesSalmonella-host cell interactionsType III secretion systemSpecific Rho family GTPasesActin cytoskeleton remodelingDifferent Rho family GTPasesSpecific cellular responsesActin remodelingGuanosine triphosphatasesRho GTPasesSecretion systemCytoskeleton remodelingBacterial proteinsGTPasesSophisticated mechanismsHost cellsDistinct rolesBacterial pathogensCell interactionsSalmonella entericaDifferential activationCentral role
2004
Salmonella Modulates Vesicular Traffic by Altering Phosphoinositide Metabolism
Hernandez LD, Hueffer K, Wenk MR, Galán J. Salmonella Modulates Vesicular Traffic by Altering Phosphoinositide Metabolism. Science 2004, 304: 1805-1807. PMID: 15205533, DOI: 10.1126/science.1098188.Peer-Reviewed Original ResearchConceptsIntracellular replicative nicheType III secretion systemActin cytoskeleton rearrangementBacteria-containing vacuolesBacterial intracellular growthPhosphoinositide phosphataseInnate immune defenseSecretion systemReplicative nicheBacterial entryCytoskeleton rearrangementSpacious phagosomesHost cellsNonphagocytic cellsIntracellular growthImmune defenseSopBPhosphoinositide metabolismSignificant defectsSalmonella entericaVacuolesMembraneCellsNichePhagosomes
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 uptakeProteinSALMONELLA INTERACTIONS WITH HOST CELLS: Type III Secretion at Work
Galán J. SALMONELLA INTERACTIONS WITH HOST CELLS: Type III Secretion at Work. Annual Review Of Cell And Developmental Biology 2001, 17: 53-86. PMID: 11687484, DOI: 10.1146/annurev.cellbio.17.1.53.Peer-Reviewed Original ResearchConceptsBacterial proteinsBacterial pathogen Salmonella entericaHost cellsType III secretion systemActin cytoskeleton dynamicsType III secretionHost cell functionsPathogen Salmonella entericaMolecular tinkeringConvergent evolutionEndocytic traffickingCytoskeleton dynamicsSpecialized organellesCellular functionsSecretion systemMicrobial pathogenesisRemarkable pathogenHost proteinsSalmonella interactionsVertebrate hostsProteinRemarkable arrayCoordinated actionCell functionSalmonella entericaMaintenance 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 interfaceSalmonella entry into host cells: the work in concert of type III secreted effector proteins
Zhou D, Galán J. Salmonella entry into host cells: the work in concert of type III secreted effector proteins. Microbes And Infection 2001, 3: 1293-1298. PMID: 11755417, DOI: 10.1016/s1286-4579(01)01489-7.Peer-Reviewed Original ResearchConceptsActin cytoskeleton rearrangementCytoskeleton rearrangementActin dynamicsHost cellsHost actin dynamicsHost signal transductionType III secretion systemActin-binding proteinsSPI-1 type III secretion systemEffector proteinsSecretion systemSignal transductionActin rearrangementBacterial proteinsSalmonella entryIntestinal epithelial cellsBacterial uptakeCdc42Coordinated stepsProteinEpithelial cellsRacRearrangementCellsTransductionCharacterization of the mutS-proximal region of the Salmonella typhimurium SPI-1 identifies a group of pathogenicity island-associated genes
Pancetti A, Galán J. Characterization of the mutS-proximal region of the Salmonella typhimurium SPI-1 identifies a group of pathogenicity island-associated genes. FEMS Microbiology Letters 2001, 197: 203-208. PMID: 11313135, DOI: 10.1111/j.1574-6968.2001.tb10604.x.Peer-Reviewed Original ResearchConceptsPathogenicity islandSecretion systemType III protein secretion systemSPI-1Type III secretion systemHigher eukaryotic hostsProtein secretion systemSet of genesIron uptake systemExpression of genesSegment of DNAPotential pathogenicity islandsEukaryotic hostsFhlA geneGene blockCentisome 63Pig genesFunctional copyTranscription factorsSalmonella chromosomeUnknown functionUptake systemGenesBacterial pathogensHomolog
2000
Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
Kubori T, Sukhan A, Aizawa S, Galán J. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 10225-10230. PMID: 10944190, PMCID: PMC27824, DOI: 10.1073/pnas.170128997.Peer-Reviewed Original ResearchConceptsType III secretion systemProtein secretion systemSecretion systemNeedle complexType III protein secretion systemHost cellular functionsSpecialized protein secretion systemType III secretion export apparatusType III secretionPathogenicity island 1Secretion complexPathogen's benefitExport apparatusCellular functionsAnimal cellsNeedle-like projectionsBacterial proteinsBacterium's abilityNeedle substructureIsland 1Host cellsMolecular characterizationNonphagocytic cellsNeedle componentBacterial pathogensStriking a balance: Modulation of the actin cytoskeleton by Salmonella
Galán J, Zhou D. Striking a balance: Modulation of the actin cytoskeleton by Salmonella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 8754-8761. PMID: 10922031, PMCID: PMC34008, DOI: 10.1073/pnas.97.16.8754.Peer-Reviewed Original ResearchConceptsType III secretion systemSecretion systemHost cellsBacterial entryGTP-binding protein Cdc42Bacterial effector proteinsInositol polyphosphate phosphatasePathogen/host relationshipActin cytoskeleton rearrangementHost cell cytosolStimulation of Cdc42Protein Cdc42Effector proteinsActin cytoskeletonExchange factorSpecialized organellesSalmonella proteinsCytoskeleton rearrangementT-plastinHost relationshipsCell cytosolF-actinCellular responsesG proteinsCdc42The Flagellar Sigma Factor FliA (ς28) Regulates the Expression of Salmonella Genes Associated with the Centisome 63 Type III Secretion System
Eichelberg K, Galán J. The Flagellar Sigma Factor FliA (ς28) Regulates the Expression of Salmonella Genes Associated with the Centisome 63 Type III Secretion System. Infection And Immunity 2000, 68: 2735-2743. PMID: 10768967, PMCID: PMC97482, DOI: 10.1128/iai.68.5.2735-2743.2000.Peer-Reviewed Original ResearchConceptsType III secretion systemSecretion systemExpression of componentsRegulatory proteinsType III protein secretion systemRegulatory mechanismsSerovar TyphimuriumFlagellar sigma factor FliASigma factor FliAProtein secretion systemTranscriptional regulatory proteinsSalmonella pathogenicity island 1Complex regulatory mechanismsFlagellar regulatory genesPathogenicity island 1Macrophage cell deathEffects of mutationsType III systemCultured epithelial cellsFlagellar genesEnterica serovar TyphimuriumMild centrifugal forceRegulatory genesSalmonella genesS. enterica serovar TyphimuriumComplex Function for SicA, a Salmonella enterica Serovar Typhimurium Type III Secretion-Associated Chaperone
Tucker S, Galán J. Complex Function for SicA, a Salmonella enterica Serovar Typhimurium Type III Secretion-Associated Chaperone. Journal Of Bacteriology 2000, 182: 2262-2268. PMID: 10735870, PMCID: PMC111276, DOI: 10.1128/jb.182.8.2262-2268.2000.Peer-Reviewed Original Research
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 invasionCytosolBacteriumSPTPAn invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contactDifferential Regulation of Salmonella typhimurium Type III Secreted Proteins by Pathogenicity Island 1 (SPI-1)-Encoded Transcriptional Activators InvF and HilA
Eichelberg K, Galán J. Differential Regulation of Salmonella typhimurium Type III Secreted Proteins by Pathogenicity Island 1 (SPI-1)-Encoded Transcriptional Activators InvF and HilA. Infection And Immunity 1999, 67: 4099-4105. PMID: 10417179, PMCID: PMC96710, DOI: 10.1128/iai.67.8.4099-4105.1999.Peer-Reviewed Original ResearchConceptsExpression of componentsSPI-1Secretion systemRegulatory proteinsType III protein secretion systemType III secretion machineryCellular responsesHost cellsFunction mutationsType III secretion systemInvasion-associated type III secretion systemProtein secretion systemTranscriptional regulatory proteinsComplex regulatory mechanismsPathogenicity island 1Secretion machineryCentisome 63Different genesRegulatory mechanismsMutant strainPathogenicity islandInvFIsland 1Differential regulationProteinCharacterization of SprA, an AraC‐like transcriptional regulator encoded within the Salmonella typhimurium pathogenicity island 1
Eichelberg K, Hardt W, Galán J. Characterization of SprA, an AraC‐like transcriptional regulator encoded within the Salmonella typhimurium pathogenicity island 1. Molecular Microbiology 1999, 33: 139-152. PMID: 10411731, DOI: 10.1046/j.1365-2958.1999.01458.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAraC Transcription FactorBacterial ProteinsBiological TransportCells, CulturedChromosome MappingChromosomes, BacterialConsensus SequenceDNA-Binding ProteinsEpithelial CellsGene Expression Regulation, BacterialGenes, BacterialGenes, ReporterHelix-Loop-Helix MotifsMolecular Sequence DataMultigene FamilyPhylogenyRecombinant Fusion ProteinsRepressor ProteinsSalmonella typhimuriumSequence AlignmentSequence Homology, Amino AcidSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticVirulenceConceptsType III secretion systemTranscriptional regulatory proteinsPathogenicity island 1Secretion systemRegulatory proteinsType III protein secretion systemSPI-1Island 1Host cellsProtein secretion systemTranscriptional regulatory cascadeSpecific transcriptional regulatory proteinsAdditional regulatory proteinsSignificant sequence similarityAraC-like transcriptional regulatorActin cytoskeletal rearrangementRegulation of expressionInvasion-associated genesExpression of genesNon-phagocytic cellsCentisome 63Effector proteinsTranscriptional regulatorsRegulatory cascadeSequence similarityType III Secretion Machines: Bacterial Devices for Protein Delivery into Host Cells
Galán J, Collmer A. Type III Secretion Machines: Bacterial Devices for Protein Delivery into Host Cells. Science 1999, 284: 1322-1328. PMID: 10334981, DOI: 10.1126/science.284.5418.1322.Peer-Reviewed Original ResearchConceptsSecretion systemComplex protein secretion systemsHost cellsType III secretion systemBacterial effector proteinsProtein secretion systemAnimal pathogenic bacteriaHost cellular functionsGram-negative pathogenic bacteriaBacterial devicesPathogenic bacteriaEffector proteinsCellular functionsFlagellar apparatusBacterial speciesEffector moleculesProtein deliveryBacteriaCellsNovel preventionBiologySpeciesPlantsProteinTherapeutic approachesRequirement of p21-activated Kinase (PAK) for Salmonella typhimurium–induced Nuclear Responses
Chen L, Bagrodia S, Cerione R, Galán J. Requirement of p21-activated Kinase (PAK) for Salmonella typhimurium–induced Nuclear Responses. Journal Of Experimental Medicine 1999, 189: 1479-1488. PMID: 10224288, PMCID: PMC2193063, DOI: 10.1084/jem.189.9.1479.Peer-Reviewed Original ResearchConceptsP21-activated kinaseBacterial effector proteinsEffector proteinsTarget proteinsSmall molecular weight GTPasesSerine/threonine kinaseType III secretion systemCdc42 effector proteinsC-Jun NH2-terminal kinase activationCdc42/RacFunction of Cdc42PAK kinase activityDedicated type III secretion systemEffector loop mutantsActin cytoskeleton rearrangementActin cytoskeleton reorganizationHost cell cytoplasmCultured epithelial cellsNuclear responseWeight GTPasesThreonine kinaseRho familyRho GTPasesSecretion systemCytoskeletal rearrangements
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 typhimurium
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