2024
Loss of function of metabolic traits in typhoidal Salmonella without apparent genome degradation
Machado L, Galán J. Loss of function of metabolic traits in typhoidal Salmonella without apparent genome degradation. MBio 2024, 15: e00607-24. PMID: 38572992, PMCID: PMC11077982, DOI: 10.1128/mbio.00607-24.Peer-Reviewed Original ResearchConceptsSalmonella enterica</i> serovar TyphiAdaptive convergent evolutionFunction of metabolic pathwaysAmino acid substitutionsConvergent evolutionMetabolic pathwaysParatyphi A.Paratyphi AHuman hostTranscriptional regulationAcid substitutionsMetabolic capabilitiesPoint mutationsParatyphoid feverTranscriptional regulatory proteinsMetabolic enzymesAffecting different genesPresence of point mutationsGenome degradationTyphoidal SalmonellaGlucose-6-phosphateCoding sequenceBioinformatics approachTyphiBacterial pathogens
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
2001
Maintenance 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 interfaceCdtA, 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 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
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 ResearchConceptsPlant 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
CROSS-TALK BETWEEN BACTERIAL PATHOGENS AND THEIR HOST CELLS
Galán J, Bliska J. CROSS-TALK BETWEEN BACTERIAL PATHOGENS AND THEIR HOST CELLS. Annual Review Of Cell And Developmental Biology 1996, 12: 221-255. PMID: 8970727, DOI: 10.1146/annurev.cellbio.12.1.221.Peer-Reviewed Original ResearchConceptsHost cellsHost cell signal transduction pathwaysProtein secretion systemHost cellular functionsSpecialized protein secretion systemSignal transduction pathwaysBacterial pathogensHost cell interactionsSecretion systemTransduction pathwaysBacterial proteinsCell physiologyBiochemical interactionsDiverse groupPathogensNovel therapeutic approachesCellsProteinTranslocationBetter understandingInteractionPathwayPhysiologyTherapeutic approachesBasic aspects
1994
Interactions of bacteria with non-phagocytic cells
Galan J. Interactions of bacteria with non-phagocytic cells. Current Opinion In Immunology 1994, 6: 590-595. PMID: 7946047, DOI: 10.1016/0952-7915(94)90146-5.Peer-Reviewed Original Research