2021
How the PhoP/PhoQ System Controls Virulence and Mg2+ Homeostasis: Lessons in Signal Transduction, Pathogenesis, Physiology, and Evolution
Groisman EA, Duprey A, Choi J. How the PhoP/PhoQ System Controls Virulence and Mg2+ Homeostasis: Lessons in Signal Transduction, Pathogenesis, Physiology, and Evolution. Microbiology And Molecular Biology Reviews 2021, 85: 10.1128/mmbr.00176-20. PMID: 34191587, PMCID: PMC8483708, DOI: 10.1128/mmbr.00176-20.Peer-Reviewed Original ResearchConceptsPhoP/PhoQ systemPhoP/PhoQSignal transductionAbundance of hundredsGram-negative bacterial speciesTwo-component systemSalmonella enterica serovar TyphimuriumRegulatory RNAsEnterica serovar TyphimuriumTranscription factorsProtease regulatorsTranscriptional effectsCationic antimicrobial peptidesInducing conditionsBacterial speciesSerovar TyphimuriumPhysiological consequencesAntimicrobial peptidesPhoQTransductionVirulenceHomeostasisAbundanceNovel formPhoP
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
2009
Activated by Different Signals, the PhoP/PhoQ Two-Component System Differentially Regulates Metal Uptake
Choi E, Groisman EA, Shin D. Activated by Different Signals, the PhoP/PhoQ Two-Component System Differentially Regulates Metal Uptake. Journal Of Bacteriology 2009, 191: 7174-7181. PMID: 19801407, PMCID: PMC2786564, DOI: 10.1128/jb.00958-09.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesBacterial ProteinsBiological TransportBlotting, WesternCation Transport ProteinsGene Expression Regulation, BacterialHydrogen-Ion ConcentrationMagnesiumMembrane Transport ProteinsMetalsPhosphorylationReverse Transcriptase Polymerase Chain ReactionSalmonella typhimuriumConceptsPhoP/PhoQ systemPhoP/PhoQTwo-component systemTwo-component regulatory systemMgtA genePhoP proteinVirulence functionsMgtA transcriptionSalmonella genesLeader regionTransporter geneBiological consequencesGenesRegulatory systemAntimicrobial peptidesDistinct setsPhoQTranscriptionMetal uptakeSalmonella entericaMultiple signalsProteinExpressionPhoPMgtA
2004
Transcriptional 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
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 cellsPhagosomes
1997
The 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
1994
A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium.
Parra‐Lopez C, Lin R, Aspedon A, Groisman EA. A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium. The EMBO Journal 1994, 13: 3964-3972. PMID: 8076592, PMCID: PMC395316, DOI: 10.1002/j.1460-2075.1994.tb06712.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBiological TransportCarrier ProteinsCloning, MolecularDrug Resistance, MicrobialMelittenMembrane ProteinsMolecular Sequence DataNADPeptidesPotassiumProtaminesReceptor, trkARecombinant ProteinsRestriction MappingSalmonella typhimuriumSequence Analysis, DNASequence Homology, Amino AcidConceptsE. coli proteinsAntimicrobial peptidesMolecular genetic analysisAntimicrobial peptide protaminePutative transportersTransport of peptidesColi proteinsSingle mutantsSalmonella proteinsSame resistance pathwaysSAP mutantsHost defense moleculesGenetic analysisDefense moleculesLoci participateChannel proteinsExhibit hypersensitivityEfflux proteinsUptake systemResistance pathwaysMutantsEscherichia coliProteinTransport of potassiumHost tissuesThe 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 Research
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 cells
1992
Resistance to host antimicrobial peptides is necessary for Salmonella virulence.
Groisman EA, Parra-Lopez C, Salcedo M, Lipps CJ, Heffron F. Resistance to host antimicrobial peptides is necessary for Salmonella virulence. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 11939-11943. PMID: 1465423, PMCID: PMC50673, DOI: 10.1073/pnas.89.24.11939.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiological EvolutionBlood ProteinsChromosome MappingCytoplasmic GranulesDefensinsGenes, BacterialGenotypeGranulocytesHumansIn Vitro TechniquesMagaininsMiceMutagenesisPeptidesProtaminesSalmonella InfectionsSalmonella typhimuriumXenopus ProteinsConceptsDifferent phenotypic classesTransposon insertion mutantsHost defense strategiesSalmonella virulence genesBacterium Salmonella typhimuriumResistance mechanismsAntimicrobial peptidesDefensin NP-1Antimicrobial peptide protamineInsertion mutantsResistance lociHost antimicrobial peptidesSalmonella virulencePhenotypic classesMutantsSuccessful pathogenDefective lipopolysaccharideAntibacterial peptidesVirulence genesPeptide mastoparanCecropin P1Defense strategiesUbiquitous typeVirulence propertiesGenes