2023
Parkinson’s disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella
Lian H, Park D, Chen M, Schueder F, Lara-Tejero M, Liu J, Galán J. Parkinson’s disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella. Nature Microbiology 2023, 8: 1880-1895. PMID: 37640963, PMCID: PMC10962312, DOI: 10.1038/s41564-023-01459-y.Peer-Reviewed Original ResearchConceptsLeucine-rich repeat kinase 2Loss of LRRK2Host defense mechanismsKinase leucine-rich repeat kinase 2Parkinson's disease-associated leucine-rich repeat kinase 2Host defense pathwaysBacterial pathogen SalmonellaRepeat kinase 2Salmonella infectionSalmonella-containing vacuolesCell-intrinsic defenseIntracellular pathogensIntracellular SalmonellaFirst lineSalmonella replicationSalmonella mutantsKinase 2Pathogen SalmonellaDefense mechanismsSalmonellaHost mitochondriaDefense pathwaysDeliveryDefense responsesCells
2006
Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis
Lara-Tejero M, Sutterwala FS, Ogura Y, Grant EP, Bertin J, Coyle AJ, Flavell RA, Galán J. Role of the caspase-1 inflammasome in Salmonella typhimurium pathogenesis. Journal Of Experimental Medicine 2006, 203: 1407-1412. PMID: 16717117, PMCID: PMC2118315, DOI: 10.1084/jem.20060206.Peer-Reviewed Original Research
2003
A Salmonella protein causes macrophage cell death by inducing autophagy
Hernandez LD, Pypaert M, Flavell RA, Galán J. A Salmonella protein causes macrophage cell death by inducing autophagy. Journal Of Cell Biology 2003, 163: 1123-1131. PMID: 14662750, PMCID: PMC2173598, DOI: 10.1083/jcb.200309161.Peer-Reviewed Original ResearchConceptsMembrane fusion activityCell deathType III protein secretion systemFusion activityProtein secretion systemMacrophage cell deathEndoplasmic reticulum markerSalmonella-infected macrophagesSecretion systemSalmonella proteinsAutophagic vesiclesMutant formsSipBHost cellsCultured cellsMitochondriaMembrane structureSalmonella entericaProteinCausative agentMarked accumulationMacrophagesCellsAutophagosomesAutophagy
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 IIISalmonella 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
Developmental Control of Endocytosis in Dendritic Cells by Cdc42
Garrett W, Chen L, Kroschewski R, Ebersold M, Turley S, Trombetta S, Galán J, Mellman I. Developmental Control of Endocytosis in Dendritic Cells by Cdc42. Cell 2000, 102: 325-334. PMID: 10975523, DOI: 10.1016/s0092-8674(00)00038-6.Peer-Reviewed Original Research
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 systemA 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 moleculesYopJ 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 techniquesMutationsA 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
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