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
A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
Zhou D, Chen L, Hernandez L, Shears S, Galán J. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Molecular Microbiology 2001, 39: 248-260. PMID: 11136447, DOI: 10.1046/j.1365-2958.2001.02230.x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBacterial ProteinsCdc42 GTP-Binding ProteinCell MembraneCells, CulturedChlorocebus aethiopsCOS CellsCytoskeletonHumansInositol PhosphatesIntestinesJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesPhosphoric Monoester HydrolasesPhosphorylationSalmonella InfectionsSalmonella typhimuriumTransfectionConceptsActin cytoskeleton rearrangementCytoskeleton rearrangementBacterial entrySecretion systemBacterial internalizationCellular responsesHost cellsRho GTPases signalingProtein secretion systemHost cell actin cytoskeleton rearrangementsHost cellular functionsSpecialized protein secretion systemCdc42-dependent mannerNon-phagocytic cellsBacterial effectorsAbility of SalmonellaInositol phosphataseCellular functionsDefective mutantsBacterial proteinsCo-ordinated functionSalmonella pathogenicityBacterium's abilitySopBPhospholipase C.
2000
Biophysical characterization of SipA, an actin‐binding protein from Salmonella enterica
Mitra K, Zhou D, Galán J. Biophysical characterization of SipA, an actin‐binding protein from Salmonella enterica. FEBS Letters 2000, 482: 81-84. PMID: 11018527, DOI: 10.1016/s0014-5793(00)02040-8.Peer-Reviewed Original ResearchConceptsActin dynamicsCoiled-coil domainF-actin stabilityActin-binding proteinsActin cytoskeleton reorganizationNon-phagocytic cellsBacterial entryCytoskeleton reorganizationAdjacent actin monomersC-terminal fragmentBiophysical characterizationF-actinCellular responsesHost cellsBacterial uptakeActin monomersProteinSalmonella entericaHelical conformationSalmonella enterica infectionsIntestinal epitheliumEnterica infectionsEssential stepSIPACellsStriking a balance: Modulation of the actin cytoskeleton by Salmonella
Galán J, Zhou D. Striking a balance: Modulation of the actin cytoskeleton by Salmonella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 8754-8761. PMID: 10922031, PMCID: PMC34008, DOI: 10.1073/pnas.97.16.8754.Peer-Reviewed Original ResearchConceptsType III secretion systemSecretion systemHost cellsBacterial entryGTP-binding protein Cdc42Bacterial effector proteinsInositol polyphosphate phosphatasePathogen/host relationshipActin cytoskeleton rearrangementHost cell cytosolStimulation of Cdc42Protein Cdc42Effector proteinsActin cytoskeletonExchange factorSpecialized organellesSalmonella proteinsCytoskeleton rearrangementT-plastinHost relationshipsCell cytosolF-actinCellular responsesG proteinsCdc42
1999
An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin
Zhou D, Mooseker M, Galán J. An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 10176-10181. PMID: 10468582, PMCID: PMC17862, DOI: 10.1073/pnas.96.18.10176.Peer-Reviewed Original ResearchConceptsActin-bundling activityT-plastinBacterial-host cell contactHost cell signal transduction pathwaysHost cellsType III secretion systemBacterial effector proteinsActin-binding proteinsSignal transduction pathwaysBacterial effectorsMembrane rufflesEffector proteinsActin cytoskeletonMembrane rufflingSecretion systemSalmonella proteinsBacterial entryBacterial internalizationSalmonella entrySignaling processesActin filamentsF-actinNonphagocytic cellsProteinCell contact
1998
A 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
1997
The invasion‐associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell
Collazo C, Galán J. The invasion‐associated type III system of Salmonella typhimurium directs the translocation of Sip proteins into the host cell. Molecular Microbiology 1997, 24: 747-756. PMID: 9194702, DOI: 10.1046/j.1365-2958.1997.3781740.x.Peer-Reviewed Original ResearchConceptsProtein secretion systemProtein translocationHost cellsSIP proteinHenle-407 cellsType III protein secretion systemType III secretion systemType III secretion apparatusType III systemSubset of targetsCentisome 63Secretion apparatusSecretion systemBacterial entryBacterial internalizationNull mutationSalmonella typhimuriumCytochalasin DTranslocation processTranslocationProteinMutationsPresence of gentamicinSipBS. typhimurium strain
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
1993
Signal transduction and invasion of epithelial cells by S. typhimurium
Pace J, Hayman M, Galán J. Signal transduction and invasion of epithelial cells by S. typhimurium. Cell 1993, 72: 505-514. PMID: 8382566, DOI: 10.1016/0092-8674(93)90070-7.Peer-Reviewed Original ResearchMeSH KeywordsArachidonate 5-LipoxygenaseArachidonic AcidCalciumCalcium-Calmodulin-Dependent Protein KinasesCells, CulturedEndocytosisEpidermal Growth FactorEpitheliumErbB ReceptorsPhospholipases APhospholipases A2PhosphorylationProtein KinasesSalmonella InfectionsSalmonella typhimuriumSignal TransductionSRS-AConceptsCultured epithelial cellsBacterial entryMitogen-activated protein kinaseEpithelial cellsS. typhimurium invasionS. typhimuriumEpidermal growth factor receptorSignal transductionProtein kinaseGrowth factor receptorHenle-407 cellsTyphimurium invasionHost cellsPathogenicity of SalmonellaFactor receptorInfected cellsMutantsInvasionCalcium fluxCellsPhospholipase A2TyphimuriumIntracellular calciumActivationFree intracellular calcium