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
Characterization 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
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 TransductionA Bacterial Toxin That Controls Cell Cycle Progression as a Deoxyribonuclease I-Like Protein
Lara-Tejero M, Galán J. A Bacterial Toxin That Controls Cell Cycle Progression as a Deoxyribonuclease I-Like Protein. Science 2000, 290: 354-357. PMID: 11030657, DOI: 10.1126/science.290.5490.354.Peer-Reviewed Original ResearchConceptsCell cycle arrestCytolethal distending toxinChromatin disruptionCycle arrestCell cycle progressionLike proteinCdtB mutantChromatin fragmentationTransient expressionMutant formsCycle progressionCell deathCDT holotoxinDistending toxinCultured cellsBacterial toxinsDeoxyribonuclease IBacterial pathogensSuch pathogensCdtBSubunitsCampylobacter jejuniToxinMorphological changesPathogensComplex 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 invasionCytosolBacteriumSPTPRole of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization
Zhou D, Mooseker M, Galán J. Role of the S. typhimurium Actin-Binding Protein SipA in Bacterial Internalization. Science 1999, 283: 2092-2095. PMID: 10092234, DOI: 10.1126/science.283.5410.2092.Peer-Reviewed Original Research
1998
YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF‐α production and downregulation of the MAP kinases p38 and JNK
Palmer L, Hobbie S, Galán J, Bliska J. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF‐α production and downregulation of the MAP kinases p38 and JNK. Molecular Microbiology 1998, 27: 953-965. PMID: 9535085, DOI: 10.1046/j.1365-2958.1998.00740.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial Outer Membrane ProteinsCalcium-Calmodulin-Dependent Protein KinasesCell LineCloning, MolecularDown-RegulationEnzyme ActivationGene Expression Regulation, BacterialGenetic Complementation TestImmunoblottingJNK Mitogen-Activated Protein KinasesLipopolysaccharidesMacrophagesMiceMitogen-Activated Protein KinasesMutationP38 Mitogen-Activated Protein KinasesTumor Necrosis Factor-alphaYersinia pseudotuberculosisConceptsY. pseudotuberculosisTNF-alpha productionMitogen-activated protein kinaseType III pathwayWild-type Y. pseudotuberculosisWild-type strainTNF-alphaPathogenic Yersinia sppYop genesYop proteinsYop secretionProtein kinaseMAP kinaseTranslational levelMutantsExposure of macrophagesYopJYersinia pseudotuberculosisSustained activationMacrophage TNF-α productionJNKP38Yersinia sppTumor necrosis factor alphaJ774A.1 murine macrophages
1996
Salmonella spp. are cytotoxic for cultured macrophages
Chen L, Kaniga K, Galán J. Salmonella spp. are cytotoxic for cultured macrophages. Molecular Microbiology 1996, 21: 1101-1115. PMID: 8885278, DOI: 10.1046/j.1365-2958.1996.471410.x.Peer-Reviewed Original ResearchConceptsProtein secretion systemNon-phagocytic cellsBacterial internalizationType III protein secretion systemCell deathFragmentation of chromatinWild-type Salmonella typhimuriumMacrophage cell deathBone marrow-derived murine macrophagesMurine macrophagesFeatures of apoptosisCentisome 63Membrane rufflingSecretion apparatusMembrane blebbingBacterial entrySalmonella chromosomeMacrophage cytotoxicityHost rangeCytoplasmic nucleosomesApoptotic bodiesBacterial uptakeCytochalasin DBiochemical techniquesMutations
1992
Involvement of the epidermal growth factor receptor in the invasion of cultured mammalian cells by Salmonella typhimurium
Galán J, Pace J, Hayman M. Involvement of the epidermal growth factor receptor in the invasion of cultured mammalian cells by Salmonella typhimurium. Nature 1992, 357: 588-589. PMID: 1608468, DOI: 10.1038/357588a0.Peer-Reviewed Original ResearchConceptsHenle-407 cellsEpidermal growth factor receptorMammalian cellsGrowth factor receptorTyrosine phosphorylationCultured mammalian cellsProtein tyrosine phosphorylationFactor receptorInternalization of SalmonellaCell surface receptorsCultured epithelial cellsAddition of EGFSuch phosphorylationSignal transductionSalmonella genesSalmonella typhimuriumEGF receptorS. typhimuriumIsogenic strainsEscherichia coliPhosphorylationEpithelial cellsGenesInternalizationInvasion
1989
Virulence and vaccine potential of phoP mutants of Salmonella typhimurium
Galán J, Curtiss R. Virulence and vaccine potential of phoP mutants of Salmonella typhimurium. Microbial Pathogenesis 1989, 6: 433-443. PMID: 2671582, DOI: 10.1016/0882-4010(89)90085-5.Peer-Reviewed Original ResearchConceptsDelayed-type hypersensitivity responseBALB/c miceProtective immune responseVirulent S. typhimuriumHypersensitivity responseC micePeyer's patchesImmune responseVaccine potentialImmunized animalsSalmonella antigensSR-11Lethal dosesPhoP mutantDosesS. typhimuriumVirulent parentSalmonella typhimuriumAvirulent mutantsLow levelsAnimalsDaysImmunizationTyphimuriumSpleen