2001
Common and Contrasting Themes of Plant and Animal Diseases
Staskawicz B, Mudgett M, Dangl J, Galan J. Common and Contrasting Themes of Plant and Animal Diseases. Science 2001, 292: 2285-2289. PMID: 11423652, DOI: 10.1126/science.1062013.Peer-Reviewed Original ResearchConceptsHost-pathogen interactionsStudy of plantsDefense signalingHost defense responsesAnimal diseasesDefense responsesEffector proteinsAnimal pathogenesisBacterial pathogenesisPathogen virulencePathogen recognitionMolecular eventsHost resistancePlantsRecent studiesBacterial colonizationSignalingVirulenceProteinColonizationHostMechanismFuture studiesPathogenesisIn Vitro Transposition System for Efficient Generation of Random Mutants of Campylobacter jejuni
Colegio O, Griffin T, Grindley N, Galán J. In Vitro Transposition System for Efficient Generation of Random Mutants of Campylobacter jejuni. Journal Of Bacteriology 2001, 183: 2384-2388. PMID: 11244083, PMCID: PMC95150, DOI: 10.1128/jb.183.7.2384-2388.2001.Peer-Reviewed Original Research
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 changesPathogensMolecular 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 pathogens
1999
Characterization 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 similaritySalmonella typhimurium Encodes a Putative Iron Transport System within the Centisome 63 Pathogenicity Island
Zhou D, Hardt W, Galán J. Salmonella typhimurium Encodes a Putative Iron Transport System within the Centisome 63 Pathogenicity Island. Infection And Immunity 1999, 67: 1974-1981. PMID: 10085045, PMCID: PMC96555, DOI: 10.1128/iai.67.4.1974-1981.1999.Peer-Reviewed Original ResearchConceptsIron transport systemPathogenicity islandGrowth defectMinimal mediumPutative periplasmic binding proteinFur-dependent mannerPutative iron transport systemApparent growth defectS. typhimurium chromosomePeriplasmic binding proteinATP-binding proteinIron uptake systemOpen reading frameWild-type S. typhimuriumIron-restricted environmentNucleotide compositionPutative permeasesTransport systemExtensive homologyABC transportersReading frameSalmonella typhimuriumVirulence phenotypesUptake systemBinding protein
1998
Identification 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 typhimuriumA substrate of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage
Hardt W, Urlaub H, Galán J. A substrate of the centisome 63 type III protein secretion system of Salmonella typhimurium is encoded by a cryptic bacteriophage. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 2574-2579. PMID: 9482928, PMCID: PMC19418, DOI: 10.1073/pnas.95.5.2574.Peer-Reviewed Original ResearchConceptsType III protein secretion systemType III secretion systemProtein secretion systemSecretion systemEffector proteinsInvasion-associated type III secretion systemCluster of genesTail fiber proteinHost cell cytoplasmSouthern hybridization analysisMobile genetic elementsCultured epithelial cellsInduction of apoptosisSopE proteinEnterica serovar TyphimuriumBacteriophage genesBacterial entryCytoskeletal rearrangementsS. enterica serovar TyphimuriumGenetic elementsPathogenicity islandFiber proteinHybridization analysisCell cytoplasmEffector molecules‘Avirulence genes’ in animal pathogens?
Galán J. ‘Avirulence genes’ in animal pathogens? Trends In Microbiology 1998, 6: 3-6. PMID: 9481815, DOI: 10.1016/s0966-842x(97)01183-9.Peer-Reviewed Original Research
1997
A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria
Hardt W, Galán J. A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 9887-9892. PMID: 9275221, PMCID: PMC23287, DOI: 10.1073/pnas.94.18.9887.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsMolecular Sequence DataPlantsSalmonellaSequence AlignmentSequence AnalysisSequence Homology, Amino AcidConceptsPlant pathogenic bacteriaType III protein secretion systemProtein secretion systemSecretion systemPlant pathogen Xanthomonas campestris pvPathogen Xanthomonas campestris pvType III secretion systemPathogenic bacteriaXanthomonas campestris pvAvirulence determinantEffector proteinsSequence similaritySalmonella proteinsBacterial proteinsCampestris pvPutative targetsSophisticated mechanismsHost cellsYersinia pseudotuberculosisNovel familyProteinBacterial pathogensNovel targetSalmonella entericaBacteria
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
The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins
Kaniga K, Bossio J, Galán J. The Salmonella typhimurium invasion genes invF and invG encode homologues of the AraC and PulD family of proteins. Molecular Microbiology 1994, 13: 555-568. PMID: 7997169, DOI: 10.1111/j.1365-2958.1994.tb00450.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAraC Transcription FactorBacterial Outer Membrane ProteinsBacterial ProteinsBase SequenceCells, CulturedCloning, MolecularDNA-Binding ProteinsGene Expression Regulation, BacterialGenes, BacterialMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataMutagenesisRecombinant ProteinsRepressor ProteinsRestriction MappingSalmonella typhimuriumSequence Homology, Amino AcidTranscription FactorsTranscription, GeneticVirulenceConceptsCultured epithelial cellsSalmonella typhimurium genesNon-polar mutationT7 RNA polymerase-based expression systemEpithelial cellsAraC familyTranscription regulatorsInv locusTyphimurium genesNucleotide sequenceSalmonella entryInvGExpression systemInvFGenesProteinSequenceMutationsS. typhimuriumFamilyTranslocasesSimilar sizeCellsMembersHomologues
1993
Cloning and molecular characterization of a gene involved in Salmonella adherence and invasion of cultured epithelial cells
Altmeyer R, McNern J, Bossio JC, Rosenshine I, Finlay B, Galán J. Cloning and molecular characterization of a gene involved in Salmonella adherence and invasion of cultured epithelial cells. Molecular Microbiology 1993, 7: 89-98. PMID: 8382333, DOI: 10.1111/j.1365-2958.1993.tb01100.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial AdhesionBacterial ProteinsBase SequenceCells, CulturedDNA Transposable ElementsEpithelial CellsEpitheliumGenes, BacterialMolecular Sequence DataMutagenesisPhenotypeRecombinant Fusion ProteinsSalmonellaSalmonella typhimuriumSequence Homology, Nucleic AcidVirulenceConceptsCultured epithelial cellsInvH geneT7 RNA polymerase expression systemBacterial membrane fractionsEpithelial cellsSignal sequenceExtensive homologyColony hybridization analysisNucleotide sequenceGene productsHomologous sequencesExpression systemException of strainsMolecular characterizationGenesHybridization analysisMembrane fractionCultured cellsEscherichia coliPolypeptideInsertion sequence IS3E. coliOrganismsInvHSequence
1990
Cloning and characterization of the asd gene of Salmonella typhimurium: use in stable maintenance of recombinant plasmids in Salmonella vaccine strains
Galán J, Nakayama K, Curtiss R. Cloning and characterization of the asd gene of Salmonella typhimurium: use in stable maintenance of recombinant plasmids in Salmonella vaccine strains. Gene 1990, 94: 29-35. PMID: 2227450, DOI: 10.1016/0378-1119(90)90464-3.Peer-Reviewed Original Research