2021
RNA chaperone activates Salmonella virulence program during infection
Choi J, Salvail H, Groisman EA. RNA chaperone activates Salmonella virulence program during infection. Nucleic Acids Research 2021, 49: 11614-11628. PMID: 34751407, PMCID: PMC8599858, DOI: 10.1093/nar/gkab992.Peer-Reviewed Original ResearchConceptsPhoP activationVirulence regulator PhoPWild-type virulenceBacterium Salmonella enterica serovar TyphimuriumWild-type S. typhimuriumSalmonella enterica serovar TyphimuriumRNA chaperonesEnterica serovar TyphimuriumRegulator PhoPRedundant proteinsMutant behavesVirulence programVirulence roleS. typhimuriumInside macrophagesSecondary structureSerovar TyphimuriumCritical functionsVirulence genesChaperonesPhoPMutantsRibosomesOrganismsCSPC
2019
Slow growth determines nonheritable antibiotic resistance in Salmonella enterica
Pontes MH, Groisman EA. Slow growth determines nonheritable antibiotic resistance in Salmonella enterica. Science Signaling 2019, 12 PMID: 31363068, PMCID: PMC7206539, DOI: 10.1126/scisignal.aax3938.Peer-Reviewed Original ResearchConceptsToxin-antitoxin modulesSlow growthGenetic repertoireSuch proteinsPersister formationAntibiotic-resistant mutantsParticular proteinPersister statePhysiological processesPersistent bacteriaPhenotypic changesBacterial populationsCell growthUse of antibioticsSalmonella entericaBactericidal antibioticsBacteriaProteinSmall subpopulationAbundanceUnderlying physiological processesAntibiotic resistanceGrowthMutantsOpposite changes
2016
Reducing Ribosome Biosynthesis Promotes Translation during Low Mg2+ Stress
Pontes MH, Yeom J, Groisman EA. Reducing Ribosome Biosynthesis Promotes Translation during Low Mg2+ Stress. Molecular Cell 2016, 64: 480-492. PMID: 27746019, PMCID: PMC5500012, DOI: 10.1016/j.molcel.2016.05.008.Peer-Reviewed Original ResearchConceptsSynthesis of ribosomesAmino acid abundanceExpression of proteinsPromotes TranslationAvailability of ATPRibosomal componentsRegulatory circuitsTranslational arrestCytosolic MgRRNA geneProtein synthesisRibosomesATP levelsLevels of ATPATP amountATPDivalent cationsMutantsTranscriptionNegative chargeGenesLow Mg2TranslationProteinAbundance
2015
Salmonella promotes virulence by repressing cellulose production
Pontes MH, Lee EJ, Choi J, Groisman EA. Salmonella promotes virulence by repressing cellulose production. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 5183-5188. PMID: 25848006, PMCID: PMC4413311, DOI: 10.1073/pnas.1500989112.Peer-Reviewed Original ResearchConceptsCellulose synthesisWild-type phenotypeWild-type virulenceSalmonella enterica serovar TyphimuriumCyclic diguanylateEnterica serovar TyphimuriumPathogen fitnessAbundant organic polymerMgtC geneAcute virulenceAllosteric activatorAbiotic surfacesMgtC mutantInside macrophagesMutantsVirulence determinantsSerovar TyphimuriumVirulenceCellulose productionEnvironmental insultsCellulose levelsBCSAAttenuated mutantsTraitsDiguanylateFlagella-independent surface motility in Salmonella enterica serovar Typhimurium
Park SY, Pontes MH, Groisman EA. Flagella-independent surface motility in Salmonella enterica serovar Typhimurium. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 1850-1855. PMID: 25624475, PMCID: PMC4330729, DOI: 10.1073/pnas.1422938112.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceBacterial ProteinsBase SequenceCation Transport ProteinsComputational BiologyFlagellaGene Expression Regulation, BacterialMagnesiumMembrane Transport ProteinsMitochondrial Proton-Translocating ATPasesMolecular Sequence DataMovementMutagenesisSalmonella typhimuriumSequence AlignmentSequence Analysis, DNAConceptsSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumPhoP/PhoQ regulatory systemMgtC mutantFlagellum-independent mannerFlagella-mediated motilitySerovar TyphimuriumForm of motilityWild-type SalmonellaNull mutantsMultiprotein complexesMgtC proteinF1Fo-ATPaseHeterologous promoterSmall proteinsUnknown functionProteinase K treatmentSurface motilityMgtAMutantsGroup motilityAllelic formsRegulatory systemBacterial replicationGenes
2013
The lipopolysaccharide modification regulator PmrA limits Salmonella virulence by repressing the type three-secretion system Spi/Ssa
Choi J, Groisman EA. The lipopolysaccharide modification regulator PmrA limits Salmonella virulence by repressing the type three-secretion system Spi/Ssa. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 9499-9504. PMID: 23690578, PMCID: PMC3677452, DOI: 10.1073/pnas.1303420110.Peer-Reviewed Original ResearchConceptsPmrA proteinNull mutantsSalmonella virulenceThree secretion systemVirulence regulatory genesSalmonella enterica serovar TyphimuriumWild-type SalmonellaEnterica serovar TyphimuriumPmrA mutantRegulatory genesProtein bindsModification genesMurine typhoid feverControl expressionLPS modificationsPmrA geneMutantsGenesSerovar TyphimuriumPathogen persistenceAntimicrobial peptidesHost tissuesPromoterVirulenceProtein
2012
Expression of STM4467-Encoded Arginine Deiminase Controlled by the STM4463 Regulator Contributes to Salmonella enterica Serovar Typhimurium Virulence
Choi Y, Choi J, Groisman EA, Kang DH, Shin D, Ryu S. Expression of STM4467-Encoded Arginine Deiminase Controlled by the STM4463 Regulator Contributes to Salmonella enterica Serovar Typhimurium Virulence. Infection And Immunity 2012, 80: 4291-4297. PMID: 23006851, PMCID: PMC3497419, DOI: 10.1128/iai.00880-12.Peer-Reviewed Original ResearchConceptsCarbamate kinaseOrnithine transcarbamoylaseArginine deiminaseSalmonella enterica Serovar Typhimurium VirulenceBacterium Salmonella enterica serovar TyphimuriumSalmonella enterica serovar TyphimuriumGene functionEnterica serovar TyphimuriumDeletion mutantsMammalian hostsPathway genesRegulatory proteinsADI systemSuccessful infectionTyphimurium virulenceS. typhimuriumMetabolic functionsGenesSerovar TyphimuriumADI activityMurine macrophagesVirulenceMutantsCertain pathogensExpression
2006
Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
Nishino K, Hsu FF, Turk J, Cromie MJ, Wösten MM, Groisman EA. Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III). Molecular Microbiology 2006, 61: 645-654. PMID: 16803591, PMCID: PMC1618816, DOI: 10.1111/j.1365-2958.2006.05273.x.Peer-Reviewed Original ResearchMeSH KeywordsAluminumBacterial ProteinsBase SequenceDrug Resistance, BacterialEscherichia coli ProteinsGene Expression Regulation, BacterialIronLipid ALipopolysaccharidesMolecular Sequence DataMutationPeriplasmPhosphoric Monoester HydrolasesPhosphorylationPolymyxin BSalmonella typhimuriumSoil MicrobiologyTranscription FactorsConceptsPmrA/PmrB systemGram-negative bacterial speciesNon-host environmentsPmrA/PmrBWild-type strainSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumOuter membraneLipopolysaccharide modificationBacterial speciesCovalent modificationResistance genesSerovar TyphimuriumOxygen-dependent killingPmrAEssential metalsHomeostatic mechanismsSalmonella survivalMutantsDephosphorylationGenesSpeciesProteinMajor constituentsIdentification
2004
Activation of the RcsC/YojN/RcsB phosphorelay system attenuates Salmonella virulence
Mouslim C, Delgado M, Groisman EA. Activation of the RcsC/YojN/RcsB phosphorelay system attenuates Salmonella virulence. Molecular Microbiology 2004, 54: 386-395. PMID: 15469511, DOI: 10.1111/j.1365-2958.2004.04293.x.Peer-Reviewed Original ResearchConceptsConstitutive mutantsSalmonella virulenceNon-phagocytic cellsPhosphorelay systemWild-type SalmonellaExpression of productsVirulence functionsFull virulenceSensor geneCps operonRcsBConstitutive activationSuccessful infectionVirulence attenuationGenesVirulence factorsAberrant expressionBacterial pathogensVirulenceMutantsHost tissuesExpressionLocation-dependent mannerMutationsAttenuation phenotypeThe PmrA-Regulated pmrC Gene Mediates Phosphoethanolamine Modification of Lipid A and Polymyxin Resistance in Salmonella enterica
Lee H, Hsu FF, Turk J, Groisman EA. The PmrA-Regulated pmrC Gene Mediates Phosphoethanolamine Modification of Lipid A and Polymyxin Resistance in Salmonella enterica. Journal Of Bacteriology 2004, 186: 4124-4133. PMID: 15205413, PMCID: PMC421605, DOI: 10.1128/jb.186.13.4124-4133.2004.Peer-Reviewed Original ResearchConceptsPolymyxin B resistancePmrA mutantB resistanceInner membrane proteinLarge periplasmic regionLipid AN-terminal regionPmrC genePhosphoethanolamine modificationSalmonella entericaPeriplasmic regionTransmembrane domainDouble mutantEnzymatic domainsMembrane proteinsGene resultsAminoarabinose modificationMutantsGenesRegulatory systemAminoarabinosePmrAPolymyxin resistanceProteinAntibiotic polymyxin BTranscriptional Control of the Antimicrobial Peptide Resistance ugtL Gene by the Salmonella PhoP and SlyA Regulatory Proteins*
Shi Y, Latifi T, Cromie MJ, Groisman EA. Transcriptional Control of the Antimicrobial Peptide Resistance ugtL Gene by the Salmonella PhoP and SlyA Regulatory Proteins*. Journal Of Biological Chemistry 2004, 279: 38618-38625. PMID: 15208313, DOI: 10.1074/jbc.m406149200.Peer-Reviewed Original ResearchMeSH KeywordsAntimicrobial Cationic PeptidesBacterial ProteinsBase SequenceBeta-GalactosidaseBinding SitesBlotting, SouthernDeoxyribonuclease IGene Expression Regulation, BacterialMagaininsMagnesiumMembrane ProteinsModels, BiologicalMolecular Sequence DataMutationPeptidesPlasmidsPolymyxin BPromoter Regions, GeneticProtein BindingSalmonellaSingle-Strand Specific DNA and RNA EndonucleasesTranscription FactorsTranscription, GeneticTranscriptional ActivationXenopus ProteinsConceptsPhoP proteinSlyA mutantSlyA proteinPhoP/PhoQTranscription start siteAntimicrobial peptidesTwo-component systemMagainin 2Transcriptional activatorAbility of SalmonellaTranscriptional controlStart siteMaster regulatorRegulatory proteinsTranscriptionVirulence attenuationAntimicrobial peptide magainin 2PhoPGenesProteinPromoterMutantsSlyA.PhoQPeptides
2003
The Salmonella SpiC protein targets the mammalian Hook3 protein function to alter cellular trafficking
Shotland Y, Krämer H, Groisman EA. The Salmonella SpiC protein targets the mammalian Hook3 protein function to alter cellular trafficking. Molecular Microbiology 2003, 49: 1565-1576. PMID: 12950921, DOI: 10.1046/j.1365-2958.2003.03668.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsCell LineCyclic AMPGenes, ReporterLysosomesMacrophagesMiceMicroscopy, FluorescenceMicrotubule-Associated ProteinsMolecular Sequence DataPhagosomesProtein BindingProtein TransportRecombinant Fusion ProteinsSalmonella typhimuriumSequence Homology, Amino AcidConceptsPhagosome-lysosome fusionCellular traffickingType III secretion systemEndosome-endosome fusionDominant negative mutantCytosol of macrophagesMammalian proteinsPhenotype of cellsProtein functionGolgi morphologySecretion systemDistribution of lysosomesSpiC genePhagosomal membraneProteinMurine macrophagesTraffickingCytosolVero cellsMacrophagesCellsMutantsHook3FusionGenesMg2+ Sensing by the Mg2+ Sensor PhoQ of Salmonella enterica
Chamnongpol S, Cromie M, Groisman EA. Mg2+ Sensing by the Mg2+ Sensor PhoQ of Salmonella enterica. Journal Of Molecular Biology 2003, 325: 795-807. PMID: 12507481, DOI: 10.1016/s0022-2836(02)01268-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBase SequenceBinding SitesConserved SequenceDNA, BacterialMagnesiumMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein Structure, TertiaryRecombinant ProteinsSalmonella entericaSequence Homology, Amino AcidTranscription, GeneticConceptsTranscription of PhoPPhoQ proteinSensor PhoQPeriplasmic domainTwo-component regulatory systemResponse regulator PhoPExpression of phoPPhoP/PhoQWild-type responseWild-type abilityAmino acid residuesGram-negative speciesRegulator PhoPGene transcriptionPhoPAcid residuesTranscriptionHistidine residuesPhoQGenesAcetyl phosphateRegulatory systemProteinMutantsSalmonella enterica
2002
Conflicting needs for a Salmonella hypervirulence gene in host and non‐host environments
Mouslim C, Hilbert F, Huang H, Groisman EA. Conflicting needs for a Salmonella hypervirulence gene in host and non‐host environments. Molecular Microbiology 2002, 45: 1019-1027. PMID: 12180921, DOI: 10.1046/j.1365-2958.2002.03070.x.Peer-Reviewed Original ResearchConceptsSole carbon sourceD-Ala-D-Ala dipeptidaseNon-host environmentsNutrient-poor conditionsPathogen Salmonella entericaCarbon sourceWild-type SalmonellaPathogen fitnessFaster growth rateGenesInfected hostHypervirulence genesMutantsInnate immunitySalmonella entericaDipeptidase activityGrowth rateHostInactivationPhenotypeFitnessDipeptidasePathogensSalmonellaEntericaFe(III)‐mediated cellular toxicity
Chamnongpol S, Dodson W, Cromie MJ, Harris ZL, Groisman EA. Fe(III)‐mediated cellular toxicity. Molecular Microbiology 2002, 45: 711-719. PMID: 12139617, DOI: 10.1046/j.1365-2958.2002.03041.x.Peer-Reviewed Original ResearchConceptsIsogenic wild-type strainSignal transduction systemWild-type strainGram-negative speciesPmrA mutantOuter membraneIron-mediated toxicityTransduction systemMicrobicidal activityBacterial survivalMajor regulatorCell deathPmrA geneIron homeostasisMutantsEscherichia coliSalmonella mutantsDeleterious metalsCellular toxicitySalmonella entericaExcellent biocatalystAnaerobic conditionsGenesRegulatorSpeciesMg2+ homeostasis and avoidance of metal toxicity
Chamnongpol S, Groisman EA. Mg2+ homeostasis and avoidance of metal toxicity. Molecular Microbiology 2002, 44: 561-571. PMID: 11972791, DOI: 10.1046/j.1365-2958.2002.02917.x.Peer-Reviewed Original ResearchConceptsPhoP/PhoQ systemPhoP mutantPresence of PhoPGram-negative bacterium Salmonella entericaPhoP/PhoQBacterium Salmonella entericaTwo-component systemCorA geneCellular functionsMutantsMetal toxicityProtein levelsIntracellular levelsPhoPMgtATranscriptionSalmonella entericaMgtBLow Mg2Levels of Mg2CorAIron accumulationPhoQUncontrolled influxUptake
2000
The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri
Moss J, Fisher P, Vick B, Groisman E, Zychlinsky A. The regulatory protein PhoP controls susceptibility to the host inflammatory response in Shigella flexneri. Cellular Microbiology 2000, 2: 443-452. PMID: 11207599, DOI: 10.1046/j.1462-5822.2000.00065.x.Peer-Reviewed Original ResearchConceptsWild-type strainPhoP mutantPhoP/PhoQ systemTwo-component regulatory systemRegulatory protein PhoPHost cell phagosomesPhoP/PhoQKey virulence genesMutant bacteriaEnteric bacteriumPathogen escapeCell phagosomesHost cellsMutantsWild-type ShigellaPolymorphonuclear leucocytesRegulatory systemVirulence genesAntimicrobial moleculesAntimicrobial peptidesPhoPExtreme acidInflammatory responseEpithelial cellsPhagosomesA Signal Transduction System that Responds to Extracellular Iron
Wösten M, Kox L, Chamnongpol S, Soncini F, Groisman E. A Signal Transduction System that Responds to Extracellular Iron. Cell 2000, 103: 113-125. PMID: 11051552, DOI: 10.1016/s0092-8674(00)00092-1.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBinding SitesCarrier ProteinsDrug Resistance, MicrobialExtracellular SpaceGene Expression Regulation, BacterialIronIron-Binding ProteinsPhenotypePolymyxinsProtein Structure, TertiarySalmonella entericaSignal TransductionTranscription FactorsTranscription, GeneticTransferrin-Binding ProteinsConceptsSignal transduction systemTransduction systemTranscription of PmrAWild-type resistancePmrA/PmrBPeriplasmic domainPmrA mutantIron transporterFerritin light chainIron binding proteinAntibiotic polymyxinBinding proteinPmrB proteinIron homeostasisNovel pathwayExtracellular ironIron toxicityProteinVariety of oxidantsLight chainMutantsTranscriptionGenesOrganismsFerric iron
1999
A Salmonella virulence protein that inhibits cellular trafficking
Uchiya K, Barbieri M, Funato K, Shah A, Stahl P, Groisman E. A Salmonella virulence protein that inhibits cellular trafficking. The EMBO Journal 1999, 18: 3924-3933. PMID: 10406797, PMCID: PMC1171468, DOI: 10.1093/emboj/18.14.3924.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBiological TransportCell LineCell SurvivalCytosolEndosomesGenes, BacterialGTP-Binding ProteinsInhibitory Concentration 50Lethal Dose 50LysosomesMacrophagesMembrane FusionMiceMolecular Sequence DataMutationPhagosomesRab5 GTP-Binding ProteinsReceptors, TransferrinSalmonella entericaVirulenceConceptsType III secretion systemSecretion systemIntracellular traffickingSPI-2 pathogenicity islandTrafficking of vesiclesEndosome-endosome fusionHost cell cytosolVirulence proteinsCellular traffickingNormal traffickingSpiC geneCell cytosolPathogenicity islandSalmonella pathogenesisSpiC mutantTraffickingProteinInhibited fusionSindbis virusSalmonella entericaTransferrin receptorJ774 macrophagesMutantsEndosomesGenes
1996
Identification of a pathogenicity island required for Salmonella survival in host cells.
Ochman H, Soncini FC, Solomon F, Groisman EA. Identification of a pathogenicity island required for Salmonella survival in host cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 7800-7804. PMID: 8755556, PMCID: PMC38828, DOI: 10.1073/pnas.93.15.7800.Peer-Reviewed Original ResearchConceptsPathogenicity islandType III secretion systemSalmonella typhimurium chromosomeWild-type levelsEpithelial cell invasionWild-type strainSPI genesSecretion systemPutative regulatorHost cellsSecretory apparatusCell invasionSecreted proteaseVirulence determinantsSpi(-) mutantsGenesProteinProteaseSalmonella survivalEnteric pathogensMutantsChromosomesIslandsCulture supernatantsForms of flagellin