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 entericaVacuolesMembraneCellsNichePhagosomesDisruption of type III secretion in Salmonella enterica serovar Typhimurium by external guide sequences
McKinney JS, Zhang H, Kubori T, Galán J, Altman S. Disruption of type III secretion in Salmonella enterica serovar Typhimurium by external guide sequences. Nucleic Acids Research 2004, 32: 848-854. PMID: 14762212, PMCID: PMC373343, DOI: 10.1093/nar/gkh219.Peer-Reviewed Original Research
2001
Induction of specific CD8+ memory T cells and long lasting protection following immunization with Salmonella typhimurium expressing a lymphocytic choriomeningitis MHC class I-restricted epitope
Shams H, Poblete F, Rüssmann H, Galán J, Donis R. Induction of specific CD8+ memory T cells and long lasting protection following immunization with Salmonella typhimurium expressing a lymphocytic choriomeningitis MHC class I-restricted epitope. Vaccine 2001, 20: 577-585. PMID: 11672924, DOI: 10.1016/s0264-410x(01)00363-2.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen-Presenting CellsCD8-Positive T-LymphocytesCell LineEpitopes, T-LymphocyteFemaleHistocompatibility Antigens Class IImmunizationImmunologic MemoryLymphocytic choriomeningitis virusMiceMice, Inbred BALB CMice, Inbred C57BLSalmonella typhimuriumVaccines, SyntheticViral VaccinesConceptsMHC class ISurvival of miceProtective immunityClass ICTL responsesT cellsAntiviral CTL responsesProtective CTL responsesMemory T cellsLymphocytic choriomeningitis virus nucleoproteinAntigen delivery vectorLCMV epitopeSpecific CD8CTL activityHeterologous vaccinationVaccinationSalmonella typhimuriumPaucity of informationLethal dosesMiceImmunityCD8Oral deliveryImmunizationType IIICdtA, CdtB, and CdtC Form a Tripartite Complex That Is Required for Cytolethal Distending Toxin Activity
Lara-Tejero M, Galán J. CdtA, CdtB, and CdtC Form a Tripartite Complex That Is Required for Cytolethal Distending Toxin Activity. Infection And Immunity 2001, 69: 4358-4365. PMID: 11401974, PMCID: PMC98507, DOI: 10.1128/iai.69.7.4358-4365.2001.Peer-Reviewed Original ResearchConceptsCytolethal distending toxinTriggers cell cycle arrestActive subunitCell cycle arrestImportant bacterial pathogensTripartite complexCell cycleCDT holotoxinDistending toxinCycle arrestCDT activityCellular toxicityCdtCSubunitsBacterial pathogensRelated toxinsCdtBToxin activityB chainB subunitCdtC.Toxic activityTripartite toxinCampylobacter jejuniTarget cellsCharacterization 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
A 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 changesPathogens
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 macrophagesThe 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 ResearchConceptsActin 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
1994
Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium
Ginocchio C, Olmsted S, Wells C, Galán J. Contact with epithelial cells induces the formation of surface appendages on Salmonella typhimurium. Cell 1994, 76: 717-724. PMID: 8124710, DOI: 10.1016/0092-8674(94)90510-x.Peer-Reviewed Original ResearchConceptsCultured epithelial cellsEpithelial cellsFormation of appendagesCell-signaling eventsDe novo protein synthesisNovo protein synthesisMembrane rufflesSurface organellesBacterial internalizationBacteria Salmonella typhimuriumSalmonella typhimuriumInternalization eventsSurface appendagesHost cellsNonphagocytic cellsS. typhimuriumProtein synthesisBacterial uptakeSuch appendagesSalmonella mutantsInternalization processIntimate interactionCellsBacteriaTyphimurium
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