2021
A Primed Subpopulation of Bacteria Enables Rapid Expression of the Type 3 Secretion System in Pseudomonas aeruginosa
Lin CK, Lee DSW, McKeithen-Mead S, Emonet T, Kazmierczak B. A Primed Subpopulation of Bacteria Enables Rapid Expression of the Type 3 Secretion System in Pseudomonas aeruginosa. MBio 2021, 12: 10.1128/mbio.00831-21. PMID: 34154400, PMCID: PMC8262847, DOI: 10.1128/mbio.00831-21.Peer-Reviewed Original ResearchConceptsType 3 secretion systemSecretion systemT3SS expressionVirulence traitsSpecific virulence traitsHuman disease severityComplex nanomachinesT3SS genesP. aeruginosa cellsReproductive fitnessIsogenic cellsHeterogeneous expressionCell envelopeT3SS effectorsMotility organellesReservoir of cellsCritical virulence traitsGene expressionRegulatory mechanismsSubpopulation of cellsGram-negative pathogensFluorescent reportersDivision timeP. aeruginosaPseudomonas aeruginosa
2019
Modulation of flagellar rotation in surface-attached bacteria: A pathway for rapid surface-sensing after flagellar attachment
Schniederberend M, Williams JF, Shine E, Shen C, Jain R, Emonet T, Kazmierczak BI. Modulation of flagellar rotation in surface-attached bacteria: A pathway for rapid surface-sensing after flagellar attachment. PLOS Pathogens 2019, 15: e1008149. PMID: 31682637, PMCID: PMC6855561, DOI: 10.1371/journal.ppat.1008149.Peer-Reviewed Original ResearchConceptsFlagellar rotationSurface-attached bacteriaGram-negative opportunistic pathogen Pseudomonas aeruginosaOpportunistic pathogen Pseudomonas aeruginosaSwitch complex proteinsSingle polar flagellumBiofilm formationSurface-associated behaviorsSurface-associated structuresType IV piliPathogen Pseudomonas aeruginosaGenetic screenPolar flagellumTranscriptional programsBiofilm initiationComplex proteinsMutant bacteriaFlagellar attachmentSecond messengerP. aeruginosaFlhFBacteriaFlagellaPathwayAltered behavior
2017
Interaction of the cyclic-di-GMP binding protein FimX and the Type 4 pilus assembly ATPase promotes pilus assembly
Jain R, Sliusarenko O, Kazmierczak BI. Interaction of the cyclic-di-GMP binding protein FimX and the Type 4 pilus assembly ATPase promotes pilus assembly. PLOS Pathogens 2017, 13: e1006594. PMID: 28854278, PMCID: PMC5595344, DOI: 10.1371/journal.ppat.1006594.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCarrier ProteinsChromatography, GelCyclic GMPFimbriae, BacterialImage Processing, Computer-AssistedIntracellular Signaling Peptides and ProteinsMicroscopy, Electron, TransmissionOxidoreductasesPolymerase Chain ReactionPseudomonas aeruginosaSurface Plasmon ResonanceVirulenceVirulence FactorsConceptsT4P assemblyAssembly ATPaseTwitching motilityPoint mutant alleleBacterial cell envelopeType IVa piliGMP receptorPilus assemblyBacterial surface structuresCell envelopeFimXLocalization patternsMutant allelesSecond messengerPilBBiofilm formationATPase activityDirectional movementIntracellular levelsPilTT4PATPaseBacteriaMotilityAssembly
2015
Cross-regulation of Pseudomonas motility systems: the intimate relationship between flagella, pili and virulence
Kazmierczak BI, Schniederberend M, Jain R. Cross-regulation of Pseudomonas motility systems: the intimate relationship between flagella, pili and virulence. Current Opinion In Microbiology 2015, 28: 78-82. PMID: 26476804, PMCID: PMC4688086, DOI: 10.1016/j.mib.2015.07.017.Peer-Reviewed Original Research
2010
In Vivo Discrimination of Type 3 Secretion System-Positive and -Negative Pseudomonas aeruginosa via a Caspase-1-Dependent Pathway
Wangdi T, Mijares LA, Kazmierczak BI. In Vivo Discrimination of Type 3 Secretion System-Positive and -Negative Pseudomonas aeruginosa via a Caspase-1-Dependent Pathway. Infection And Immunity 2010, 78: 4744-4753. PMID: 20823203, PMCID: PMC2976309, DOI: 10.1128/iai.00744-10.Peer-Reviewed Original ResearchConceptsType 3 secretion systemSecretion systemInnate immune systemCaspase-1-dependent pathwayImmune systemBone marrow-derived cellsInterleukin-1 receptorPseudomonas aeruginosaMarrow-derived cellsMolecular patternsToll-like receptorsRapid inflammatory responseNegative bacteriaCaspase-1 activityPotential pathogensBacteriaMicrobesNegative Pseudomonas aeruginosaPulmonary infectionCaspase-1Inflammatory responseMutantsRapid recognitionInfectionReceptors
2009
Pseudomonas aeruginosa OspR is an oxidative stress sensing regulator that affects pigment production, antibiotic resistance and dissemination during infection
Lan L, Murray TS, Kazmierczak BI, He C. Pseudomonas aeruginosa OspR is an oxidative stress sensing regulator that affects pigment production, antibiotic resistance and dissemination during infection. Molecular Microbiology 2009, 75: 76-91. PMID: 19943895, PMCID: PMC2881571, DOI: 10.1111/j.1365-2958.2009.06955.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAnimalsAnti-Bacterial AgentsBeta-Lactam ResistanceBeta-LactamsFemaleGene DeletionGene Expression Regulation, BacterialGlutathione PeroxidaseHydrogen PeroxideMiceMice, Inbred C57BLModels, BiologicalMutagenesis, Site-DirectedOxidative StressPigments, BiologicalPneumoniaPseudomonas aeruginosaPseudomonas InfectionsQuorum SensingRepressor ProteinsSignal TransductionStress, PhysiologicalTyrosineVirulenceConceptsOxidative stress sensingCys-24Stress sensingPigment productionNull mutant strainOxidative stressSerine substitution mutantsGlobal regulatorPromoter DNASubstitution mutantsAdditional genesInside hostsQuorum sensingCys residuesMutant strainConstitutive expressionMultiple pathwaysRegulatory effectsBeta-lactam resistanceGenesSignificant inductionRegulatorTyrosine metabolismOSPRP. aeruginosa
2007
Pseudomonas aeruginosa chronic colonization in cystic fibrosis patients
Murray TS, Egan M, Kazmierczak BI. Pseudomonas aeruginosa chronic colonization in cystic fibrosis patients. Current Opinion In Pediatrics 2007, 19: 83-88. PMID: 17224667, DOI: 10.1097/mop.0b013e3280123a5d.Peer-Reviewed Original ResearchConceptsCystic fibrosis patientsChronic colonizationAcute infectionFibrosis patientsCystic fibrosisP. aeruginosaChronic pulmonary colonizationChronic pulmonary diseaseCystic fibrosis airwayHost immune systemMucoid P. aeruginosaP. aeruginosa behaviorCystic fibrosis lungPulmonary diseaseClinical benefitChronic infectionP. aeruginosa pathogenesisLeading causePulmonary colonizationNew therapiesImmune systemAggressive usePotential therapeuticsInfectionPatients
2006
Mutational Analysis of RetS, an Unusual Sensor Kinase-Response Regulator Hybrid Required for Pseudomonas aeruginosa Virulence
Laskowski MA, Kazmierczak BI. Mutational Analysis of RetS, an Unusual Sensor Kinase-Response Regulator Hybrid Required for Pseudomonas aeruginosa Virulence. Infection And Immunity 2006, 74: 4462-4473. PMID: 16861632, PMCID: PMC1539586, DOI: 10.1128/iai.00575-06.Peer-Reviewed Original ResearchConceptsType III secretion system proteinsSignal transduction domainsSecretion system proteinsUpregulation of genesPeriplasmic domainSensor kinaseReceiver domainTransmembrane domainRegulator proteinTransduction domainMutational analysisSignaling roleSystem proteinsReciprocal regulationPseudomonas aeruginosaRET activityBiofilm formationVirulence factorsOpportunistic pathogenT3SSProteinRET alleleRETP. aeruginosaKey roleAnalysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
Kazmierczak BI, Lebron MB, Murray TS. Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Molecular Microbiology 2006, 60: 1026-1043. PMID: 16677312, PMCID: PMC3609419, DOI: 10.1111/j.1365-2958.2006.05156.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell MovementCyclic GMPEscherichia coli ProteinsFemaleFimbriae, BacterialHeLa CellsHumansMiceMice, Inbred C57BLPhosphoric Diester HydrolasesPhosphorus-Oxygen LyasesPneumonia, BacterialPoint MutationProtein Structure, TertiaryPseudomonas aeruginosaSequence DeletionVirulenceConceptsEAL domainBacterial poleGGDEF-EAL proteinsCyclic dimeric guanosine monophosphateDiguanylate cyclase activityPolar surface structuresType IV piliWild-type strainGGDEF domainDiguanylate cyclasesREC domainLocalization signalPilus assemblyGGDEFNon-polar sitesFimXSurface piliPseudomonas aeruginosaPhosphodiesterase activityBiofilm formationProteinMutantsPiliMotilityDomain
2005
An indirect enzyme-linked immunosorbent assay for rapid and quantitative assessment of Type III virulence phenotypes of Pseudomonas aeruginosa isolates
Li L, Ledizet M, Kar K, Koski RA, Kazmierczak BI. An indirect enzyme-linked immunosorbent assay for rapid and quantitative assessment of Type III virulence phenotypes of Pseudomonas aeruginosa isolates. Annals Of Clinical Microbiology And Antimicrobials 2005, 4: 22. PMID: 16375761, PMCID: PMC1360672, DOI: 10.1186/1476-0711-4-22.Peer-Reviewed Original ResearchConceptsClinical isolatesEpithelial cellsOptimal treatment strategyLarge clinical studiesP. aeruginosa type III secretion systemP. aeruginosa isolatesEnzyme-linked immunosorbent assayEnzyme-linked immunosorbentType III secretion systemSecretion phenotypeIndirect enzyme-linked immunosorbentPseudomonas aeruginosaPoor outcomeInfected patientsIndirect enzyme-linked immunosorbent assayTreatment strategiesClinical studiesClinical diseaseSevere diseaseAeruginosa isolatesELISA assaysConclusionThe availabilityImmunosorbent assayCultured epithelial cellsVirulence factors
2001
INTERACTION OF BACTERIAL PATHOGENS WITH POLARIZED EPITHELIUM
Kazmierczak B, Mostov K, Engel J. INTERACTION OF BACTERIAL PATHOGENS WITH POLARIZED EPITHELIUM. Annual Review Of Microbiology 2001, 55: 407-435. PMID: 11544362, DOI: 10.1146/annurev.micro.55.1.407.Peer-Reviewed Original ResearchPseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair
Geiser T, Kazmierczak B, Garrity‐Ryan L, Matthay M, Engel J. Pseudomonas aeruginosa ExoT inhibits in vitro lung epithelial wound repair. Cellular Microbiology 2001, 3: 223-236. PMID: 11298646, DOI: 10.1046/j.1462-5822.2001.00107.x.Peer-Reviewed Original ResearchConceptsGTPase-activating proteinsEpithelial wound repairPseudomonas aeruginosa ExoTRho family GTPasesWound repairPathogen Pseudomonas aeruginosaNosocomial pathogen Pseudomonas aeruginosaP. aeruginosa internalizationEpithelial cellsP. aeruginosaGAP domainGAP activityBacterial proteinsCell roundingCytoskeleton collapseLung epithelial wound repairExoTCell detachmentVivo virulenceProteinEpithelial tissue damageImmune effector cellsLocal host defenseIntact epithelial barrierHost defense
2000
The Arginine Finger Domain of ExoT Contributes to Actin Cytoskeleton Disruption and Inhibition of Internalization ofPseudomonas aeruginosa by Epithelial Cells and Macrophages
Garrity-Ryan L, Kazmierczak B, Kowal R, Comolli J, Hauser A, Engel J. The Arginine Finger Domain of ExoT Contributes to Actin Cytoskeleton Disruption and Inhibition of Internalization ofPseudomonas aeruginosa by Epithelial Cells and Macrophages. Infection And Immunity 2000, 68: 7100-7113. PMID: 11083836, PMCID: PMC97821, DOI: 10.1128/iai.68.12.7100-7113.2000.Peer-Reviewed Original ResearchConceptsEpithelial cellsImportant nosocomial pathogenType III secretion systemHost cellsMacrophage-like cellsAcute pneumoniaMouse modelNosocomial pathogenOfPseudomonas aeruginosaType IIIJ774.1 macrophage-like cellsSecretion systemStrain PA103ExoTPseudomonas aeruginosaCellsCytoskeleton disruptionNegative regulatorPA103Reduced colonizationActin cytoskeleton disruptionPrevious studiesAeruginosaPneumoniaVirulence