1997
Regulation of polymyxin resistance and adaptation to low-Mg2+ environments
Groisman EA, Kayser J, Soncini FC. Regulation of polymyxin resistance and adaptation to low-Mg2+ environments. Journal Of Bacteriology 1997, 179: 7040-7045. PMID: 9371451, PMCID: PMC179645, DOI: 10.1128/jb.179.22.7040-7045.1997.Peer-Reviewed Original ResearchConceptsLPS modificationsAntimicrobial proteinsTranscription of PmrAPolymyxin resistanceWild-type organismsTwo-component systemExpression of pmrAAmino acid substitutionsPeptide antibiotic polymyxin BRegulatory proteinsPmrA-PmrBBacterial survivalAcid substitutionsMicromolar Mg2PmrAProteinHuman neutrophilsBacterial bindingGenesLociCationic polypeptidesAntibiotic polymyxin BOverall negative chargeSalmonella typhimuriumPhagocytic cellsThe Genetic Basis of Microbial Resistance to Antimicrobial Peptides
Groisman E, Aspedon A. The Genetic Basis of Microbial Resistance to Antimicrobial Peptides. Methods In Molecular Biology 1997, 78: 205-215. PMID: 9276306, DOI: 10.1385/0-89603-408-9:205.Peer-Reviewed Original ResearchConceptsSmall cationic peptidesAntimicrobial peptidesPathogen Salmonella typhimuriumDivergent organismsMillions of yearsMammalian hostsCationic peptidesGenetic basisAnimal hostsHost defense peptidesDiverse arrayHost tissuesInnate immunityVirulence propertiesDefense peptidesHostChemical barrierSalmonella typhimuriumMicroorganismsMicrobial resistanceS. typhimuriumPeptidesEnteric pathogensAntibiotic propertiesOpportunistic microorganisms
1996
Two-component regulatory systems can interact to process multiple environmental signals
Soncini FC, Groisman EA. Two-component regulatory systems can interact to process multiple environmental signals. Journal Of Bacteriology 1996, 178: 6796-6801. PMID: 8955299, PMCID: PMC178578, DOI: 10.1128/jb.178.23.6796-6801.1996.Peer-Reviewed Original ResearchConceptsTwo-component systemPmrA/PmrB systemTwo-component regulatory systemMultiple environmental signalsPhoP/PhoQAcid-mediated activationPmrA proteinPhoQ proteinResponse regulatorTranscriptional regulationEnvironmental signalsEnvironmental cuesTranscriptionLociRegulatory systemVirulence determinantsGenesProteinPathogenic bacteriaPhoPMild acidificationPmrASalmonella typhimuriumBroad spectrumPhoQThe antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium
Aspedon A, Groisman EA. The antibacterial action of protamine: evidence for disruption of cytoplasmic membrane energization in Salmonella typhimurium. Microbiology 1996, 142: 3389-3397. PMID: 9004502, DOI: 10.1099/13500872-142-12-3389.Peer-Reviewed Original ResearchConceptsCytoplasmic membraneNuclei of spermNutrient uptake functionsCellular ATP contentElectrical membrane potentialHigher delta psi valuesRespiring cellsLoss of viabilityMembrane energizationDifferent animal speciesProline uptakeProtein synthesisEnergy transductionMode of actionAnimal speciesUptake functionDelta psi valuesMembrane potentialCell lysisRapid effluxMechanism of actionPolycationic peptidesATP contentProtamineSalmonella typhimuriumMolecular basis of the magnesium deprivation response in Salmonella typhimurium: identification of PhoP-regulated genes
Soncini FC, Véscovi E, Solomon F, Groisman EA. Molecular basis of the magnesium deprivation response in Salmonella typhimurium: identification of PhoP-regulated genes. Journal Of Bacteriology 1996, 178: 5092-5099. PMID: 8752324, PMCID: PMC178303, DOI: 10.1128/jb.178.17.5092-5099.1996.Peer-Reviewed Original ResearchConceptsTranscription of PhoPPhoP-dependent mannerOpen reading frameLac gene fusionsWild-type strainPhoP-PhoQ systemTwo-component systemUDP-glucose dehydrogenaseSequence similarityPhoP-PhoQPhoPQ operonReading frameDeprivation responseFusion strainMolecular basisSalmonella typhimuriumPhoPDifferent proteinsSolid mediumGene fusionsUptake systemGenesNormal growthMgtASuch fusionMg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence
Véscovi E, Soncini F, Groisman E. Mg2+ as an Extracellular Signal: Environmental Regulation of Salmonella Virulence. Cell 1996, 84: 165-174. PMID: 8548821, DOI: 10.1016/s0092-8674(00)81003-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBase SequenceCationsGene Expression Regulation, BacterialHydrogen-Ion ConcentrationKineticsMagnesiumMolecular Sequence DataMutationPeptidesPhenotypeProtein ConformationSalmonella typhimuriumSensitivity and SpecificitySignal TransductionTranscription FactorsVirulenceConceptsPhoP/PhoQ systemTranscription of PhoPSignal transduction cascadeVirulence regulatory systemGene expression patternsPeriplasmic domainWild-type SalmonellaExtracellular signalsTransduction cascadeSalmonella virulenceExpression patternsFirst messengersPhoPRegulatory systemGenesPhoQSalmonella typhimuriumPhysiological concentrationsDivalent cationsTranscriptionConcentration of Mg2LociMg2DomainVirulence
1994
The role of the PhoP/PhoQ regulon in Salmonella virulence
Véscovi E, Soncini FC, Groisman EA. The role of the PhoP/PhoQ regulon in Salmonella virulence. Research In Microbiology 1994, 145: 473-480. PMID: 7855434, DOI: 10.1016/0923-2508(94)90096-5.Peer-Reviewed Original ResearchThe origin and evolution of species differences in Escherichia coli and Salmonella typhimurium
Ochman H, Groisman EA. The origin and evolution of species differences in Escherichia coli and Salmonella typhimurium. EXS 1994, 69: 479-493. PMID: 7994120, DOI: 10.1007/978-3-0348-7527-1_27.Peer-Reviewed Original ResearchConceptsSpecies-specific sequencesSalmonella chromosomeEscherichia coliCodon usage patternsOpen reading frameHost epithelial cellsCommon ancestorMap positionPhenotypic charactersReading frameBase compositionHorizontal transferSalmonella typhimuriumMutant strainGenetic differencesEnteric speciesBacterial speciesGenomePoint mutationsPhenotypic characteristicsSpeciesCorresponding regionChromosomesSpecies differencesEpithelial cells
1993
Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium.
Parra‐Lopez C, Baer MT, Groisman EA. Molecular genetic analysis of a locus required for resistance to antimicrobial peptides in Salmonella typhimurium. The EMBO Journal 1993, 12: 4053-4062. PMID: 8223423, PMCID: PMC413698, DOI: 10.1002/j.1460-2075.1993.tb06089.x.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAnti-Bacterial AgentsATP-Binding Cassette TransportersBase SequenceBiological TransportCloning, MolecularDrug Resistance, MicrobialEnterobacteriaceaeGenes, BacterialMelittenModels, BiologicalMolecular Sequence DataOperonPeptidesProtaminesSalmonella typhimuriumSequence Analysis, DNASequence Homology, Amino AcidConceptsUptake of oligopeptidesSet of genesOpen reading frameMolecular genetic analysisMammalian mdrYeast STE6Wild-type plasmidOperon structurePeriplasmic componentPeptide pheromoneNovel transporterReading frameKb segmentSalmonella typhimuriumGenetic analysisKb mRNASmall cationic peptidesSuccessful pathogenAntimicrobial peptide melittinSequence analysisCassette familyEnteric bacteriaPeptide transportAntimicrobial peptidesCancer cellsCognate gene clusters govern invasion of host epithelial cells by Salmonella typhimurium and Shigella flexneri.
Groisman EA, Ochman H. Cognate gene clusters govern invasion of host epithelial cells by Salmonella typhimurium and Shigella flexneri. The EMBO Journal 1993, 12: 3779-3787. PMID: 8404849, PMCID: PMC413660, DOI: 10.1002/j.1460-2075.1993.tb06056.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigens, BacterialAntigens, SurfaceBase SequenceBlotting, SouthernChromosomes, BacterialDNAEpithelial CellsEpitheliumGenes, BacterialGenetic Complementation TestHumansMiceMolecular Sequence DataMultigene FamilyMutationRestriction MappingSalmonella typhimuriumSequence Homology, Amino AcidShigella flexneriTumor Cells, CulturedConceptsEpithelial cellsEnteric pathogen Salmonella typhimuriumHost epithelial cellsSurface antigenSalmonella typhimuriumPathogen Salmonella typhimuriumConstellation of genesInvasion propertiesShigella flexneriVirulence plasmidShigellaVirulence attributesAntigenSalmonellaBacterial entryProtein secretion
1991
Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein
Vartak NB, Reizer J, Reizer A, Gripp JT, Groisman EA, Wu L, Tomich JM, Saier MH. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Research In Microbiology 1991, 142: 951-963. PMID: 1805309, DOI: 10.1016/0923-2508(91)90005-u.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCarrier ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsFructoseGene Expression Regulation, BacterialIn Vitro TechniquesOperator Regions, GeneticOperonPeriplasmic Binding ProteinsPromoter Regions, GeneticRepressor ProteinsRestriction MappingSalmonella typhimuriumConceptsRibose binding proteinTranscriptional regulatory proteinsN-terminal hydrophobic signal sequenceRegulatory proteinsPeriplasmic ribose-binding proteinBacterial DNA-binding proteinsHydrophobic signal sequencePeriplasmic binding proteinRibose-binding proteinDNA-binding proteinsCentral metabolic pathwaysN-terminal regionOperator-promoter regionChemoreception systemFructose operonSignature motifTranscriptional regulationRepressor functionHelix motifPhylogenetic treeSignal sequenceGene sequencesNucleotide sequenceSequence identitySalmonella typhimurium
1989
Salmonella typhimurium phoP virulence gene is a transcriptional regulator.
Groisman EA, Chiao E, Lipps CJ, Heffron F. Salmonella typhimurium phoP virulence gene is a transcriptional regulator. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 7077-7081. PMID: 2674945, PMCID: PMC297997, DOI: 10.1073/pnas.86.18.7077.Peer-Reviewed Original ResearchConceptsExpression of lociAmino acid sequenceDifferent environmental stimuliFacultative intracellular pathogenGram-negative speciesTranscriptional regulatorsYeast SaccharomycesExtensive homologyDNA sequencesGene productsAcid sequenceHost phagocytic cellsPhosphate availabilityEnvironmental stimuliIntracellular pathogensPhoP genePhoP mutationVirulence genesPhoPGenesLociSequenceSalmonella typhimuriumPhagocytic cellsPhoBA Salmonella Locus that Controls Resistance to Microbicidal Proteins from Phagocytic Cells
Fields P, Groisman E, Heffron F. A Salmonella Locus that Controls Resistance to Microbicidal Proteins from Phagocytic Cells. Science 1989, 243: 1059-1062. PMID: 2646710, DOI: 10.1126/science.2646710.Peer-Reviewed Original ResearchConceptsIntracellular pathogen Salmonella typhimuriumPhagocytic cellsImportant health problemProfessional phagocytic cellsFacultative intracellular pathogenPrimary defense mechanismHealth problemsMicrobicidal mechanismsPathogen Salmonella typhimuriumIntracellular survivalIntracellular pathogensMicrobicidal proteinsDefense mechanismsSalmonella typhimuriumCells
1987
Cloning of genes from members of the family Enterobacteriaceae with mini-Mu bacteriophage containing plasmid replicons
Groisman EA, Casadaban MJ. Cloning of genes from members of the family Enterobacteriaceae with mini-Mu bacteriophage containing plasmid replicons. Journal Of Bacteriology 1987, 169: 687-693. PMID: 3542967, PMCID: PMC211834, DOI: 10.1128/jb.169.2.687-693.1987.Peer-Reviewed Original ResearchConceptsSensitive recipient strainFamily EnterobacteriaceaeHigh phage titersC. freundiiProteus mirabilisPlasmid repliconsCitrobacter freundiiS. typhimuriumDrug-resistant transductantsSpecific mutationsMu derivativesE. coliSalmonella typhimuriumEnterobacteriaceaeFreundiiRecipient strainPhage titerTyphimuriumEscherichia coli bacteriophageInfectionTiters