2020
A Physiological Basis for Nonheritable Antibiotic Resistance
Pontes MH, Groisman EA. A Physiological Basis for Nonheritable Antibiotic Resistance. MBio 2020, 11: 10.1128/mbio.00817-20. PMID: 32546621, PMCID: PMC7298711, DOI: 10.1128/mbio.00817-20.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsAnti-Bacterial AgentsBacteriaBacterial Physiological PhenomenaDrug Resistance, Multiple, BacterialHumansMiceMicrobial Sensitivity TestsConceptsNonheritable resistanceAntibiotic toleranceCore cellular processesAcquisition of genesToxin-antitoxin modulesExpression of genesSlow bacterial growthActivity of toxinsAbility of bacteriaBacterial genomesCellular processesNutrient limitationBacterial growthGuanosine tetraphosphateGenetic changesBacterial populationsFeedback inhibitionPhysiological basisGenesOrganismsSmall subpopulationBacteriostatic antibioticsAntibiotic resistanceGenomeTolerance
2005
Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium
Nishino K, Latifi T, Groisman EA. Virulence and drug resistance roles of multidrug efflux systems of Salmonella enterica serovar Typhimurium. Molecular Microbiology 2005, 59: 126-141. PMID: 16359323, DOI: 10.1111/j.1365-2958.2005.04940.x.Peer-Reviewed Original ResearchConceptsDrug efflux systemsEfflux systemSalmonella virulenceEscherichia coli homologueToxic compound extrusionResponse regulator PhoPATP-binding cassette (ABC) superfamiliesPhoP/PhoQOuter membrane componentsAmino acid sequenceDrug resistance rolesTwo-component systemSalmonella enterica serovar TyphimuriumGram-negative speciesMultidrug efflux systemsSame operonEnterica serovar TyphimuriumRegulator PhoPCompound extrusionAcid sequenceMajor facilitatorEfflux system genesPromoter regionVirulence phenotypesMajor regulator
2004
PhoP‐regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B
Shi Y, Cromie MJ, Hsu F, Turk J, Groisman EA. PhoP‐regulated Salmonella resistance to the antimicrobial peptides magainin 2 and polymyxin B. Molecular Microbiology 2004, 53: 229-241. PMID: 15225317, DOI: 10.1111/j.1365-2958.2004.04107.x.Peer-Reviewed Original Research
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
The 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 typhimurium