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
2014
A Conservative Amino Acid Mutation in the Master Regulator FleQ Renders Pseudomonas aeruginosa Aflagellate
Jain R, Kazmierczak BI. A Conservative Amino Acid Mutation in the Master Regulator FleQ Renders Pseudomonas aeruginosa Aflagellate. PLOS ONE 2014, 9: e97439. PMID: 24827992, PMCID: PMC4020848, DOI: 10.1371/journal.pone.0097439.Peer-Reviewed Original ResearchConceptsMurine pulmonary infectionIL-1 signalPresence of mutationsPulmonary infectionAcute infectionBacterial clearanceHost responseBacterial infectionsClinical strainsInfectionSystem expressionAmino acid changesAmino acid mutationsSingle amino acid changeStrain PA103ClearanceAmino acid substitutionsPseudomonas aeruginosa pathogenesisPathogen recognitionAcid changesPA103Negative correlationMotilityAcid mutationsConservative amino acid substitutions
1993
Analysis of the structure and subcellular location of filamentous phage pIV
Russel M, Kaźmierczak B. Analysis of the structure and subcellular location of filamentous phage pIV. Journal Of Bacteriology 1993, 175: 3998-4007. PMID: 8320216, PMCID: PMC204828, DOI: 10.1128/jb.175.13.3998-4007.1993.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseBacterial ProteinsCell CompartmentationColiphagesDNA Mutational AnalysisGene Expression Regulation, BacterialGenes, ViralHeat-Shock ProteinsMembrane ProteinsMutationOperonRecombinant Fusion ProteinsSequence DeletionSequence Homology, Amino AcidSpheroplastsSubcellular FractionsViral ProteinsVirus ReplicationConceptsMembrane localization domainIntegral membrane proteinsSubstrate-binding domainAmino-terminal halfCarboxy-terminal halfSeries of genesCell fractionation studiesCytoplasmic domainPhage assemblyDeletion mutantsMembrane proteinsSubcellular locationLocalization domainFusion proteinFractionation studiesFilamentous phagePhosphatase activityFilamentous bacteriophageAlkaline phosphatase activityMissense mutationsProteinAssemblyDomainMutantsGenes