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
2012
The Carbon Monoxide Releasing Molecule CORM-2 Attenuates Pseudomonas aeruginosa Biofilm Formation
Murray TS, Okegbe C, Gao Y, Kazmierczak BI, Motterlini R, Dietrich LE, Bruscia EM. The Carbon Monoxide Releasing Molecule CORM-2 Attenuates Pseudomonas aeruginosa Biofilm Formation. PLOS ONE 2012, 7: e35499. PMID: 22563385, PMCID: PMC3338523, DOI: 10.1371/journal.pone.0035499.Peer-Reviewed Original ResearchConceptsCORM-2 treatmentP. aeruginosa lung infectionP. aeruginosaAeruginosa lung infectionCORM-2Clinical P. aeruginosaMolecule CORM-2Current antimicrobial agentsChronic infectionLung infectionNew therapiesRelated infectionsNon-mucoid strainsReactive oxygen speciesInfectionNovel therapeutic propertiesTherapeutic propertiesAntimicrobial agentsAdditive effectPseudomonas aeruginosaBiofilm formationOxygen speciesTreatmentAeruginosa
2010
Swarming motility, secretion of type 3 effectors and biofilm formation phenotypes exhibited within a large cohort of Pseudomonas aeruginosa clinical isolates
Murray TS, Ledizet M, Kazmierczak BI. Swarming motility, secretion of type 3 effectors and biofilm formation phenotypes exhibited within a large cohort of Pseudomonas aeruginosa clinical isolates. Journal Of Medical Microbiology 2010, 59: 511-520. PMID: 20093376, PMCID: PMC2855384, DOI: 10.1099/jmm.0.017715-0.Peer-Reviewed Original Research
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