2025
FlbB forms a distinctive ring essential for periplasmic flagellar assembly and motility in Borrelia burgdorferi
Botting J, Rahman M, Xu H, Yue J, Guo W, Del Mundo J, Hammel M, Motaleb M, Liu J. FlbB forms a distinctive ring essential for periplasmic flagellar assembly and motility in Borrelia burgdorferi. PLOS Pathogens 2025, 21: e1012812. PMID: 39777417, PMCID: PMC11750108, DOI: 10.1371/journal.ppat.1012812.Peer-Reviewed Original ResearchConceptsComplex protein networkPeriplasmic flagellaProtein networkB. burgdorferi mutantFlagellar motorFlat-wave morphologyStator complexLyme disease spirochete Borrelia burgdorferiGroup of bacteriaCryo-electron tomographyCollar proteinFlagellar assemblyHost infectionHuman pathogensFlbBPeriplasmic ringSpirochete Borrelia burgdorferiCollar assemblyMotilityFlagellaBorrelia burgdorferiSpirochetesMolecular modelingCollarMutants
2023
Anti-σ28 Factor FlgM Regulates Flagellin Gene Expression and Flagellar Polarity of Treponema denticola
Kurniyati K, Chang Y, Guo W, Liu J, Malkowski M, Li C. Anti-σ28 Factor FlgM Regulates Flagellin Gene Expression and Flagellar Polarity of Treponema denticola. Journal Of Bacteriology 2023, 205: e00463-22. PMID: 36715541, PMCID: PMC9945498, DOI: 10.1128/jb.00463-22.Peer-Reviewed Original ResearchConceptsFlagellin gene expressionPeriplasmic flagellaGene expressionSpirochete Treponema denticolaOral spirochete Treponema denticolaCryo-electron tomography analysisFlagellar gene expressionCore RNA polymeraseGroup of bacteriaFlgM proteinFlagellar genesBipolar flagellaHeterologous expressionDependent promotersFlagellar numberRNA polymeraseFlgMFliAMutational analysisFlagellin geneMolecular mechanismsSpirochete motilityHuman diseasesLines of evidenceEnds of cells
2022
Identification and Characterization of the Alternative σ28 Factor in Treponema denticola
Kurniyati K, Chang Y, Liu J, Li C. Identification and Characterization of the Alternative σ28 Factor in Treponema denticola. Journal Of Bacteriology 2022, 204: e00248-22. PMID: 36043861, PMCID: PMC9487585, DOI: 10.1128/jb.00248-22.Peer-Reviewed Original ResearchConceptsDependent promotersTranscription factorsSpirochete Treponema denticolaGene expressionOral spirochete Treponema denticolaCryo-electron tomography analysisFlagellin gene expressionExpression of flagellinSite-directed mutagenesisFlagellar regulationChemotaxis genesPeriplasmic flagellaRNA polymeraseFliABacterial motilityTranscriptional factorsLate promoterExternal flagellaLines of evidenceEscherichia coliPromoterT. denticolaBiochemical analysisEssential roleE. coliFliL ring enhances the function of periplasmic flagella
Guo S, Xu H, Chang Y, Motaleb MA, Liu J. FliL ring enhances the function of periplasmic flagella. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2117245119. PMID: 35254893, PMCID: PMC8931381, DOI: 10.1073/pnas.2117245119.Peer-Reviewed Original ResearchConceptsFlagellar motorBacterial motilityCryo-electron tomographyStator complexFlagellar proteinsMutant cellsPeriplasmic flagellaActive conformationSitu structureFascinating questionsSupramolecular complexesMotilityComplexesMotBOptimal functionFliLFlagellaIon fluxProteinFunctionAssemblyRemodelingCellsConformationBorrelia
2021
Characterization of the Flagellar Collar Reveals Structural Plasticity Essential for Spirochete Motility
Chang Y, Xu H, Motaleb MA, Liu J. Characterization of the Flagellar Collar Reveals Structural Plasticity Essential for Spirochete Motility. MBio 2021, 12: e02494-21. PMID: 34809456, PMCID: PMC8609358, DOI: 10.1128/mbio.02494-21.Peer-Reviewed Original ResearchConceptsLyme disease spirochete Borrelia burgdorferiPeriplasmic flagellaSpirochete motilityCryo-electron tomographySpirochete Borrelia burgdorferiRemarkable structural plasticityComplex host environmentSerious human diseasesFlagellar assemblyCollar ComplexMultiprotein complexesFlagellar collarFlagellar motorDistinct functionsDistinct morphologiesRemarkable plasticityHuman diseasesBorrelia burgdorferiHost environmentFlagellaStructural plasticityRemarkable groupMotilityProteinHost connective tissueRole of the major determinant of polar flagellation FlhG in the endoflagella‐containing spirochete Leptospira
Fule L, Halifa R, Fontana C, Sismeiro O, Legendre R, Varet H, Coppée J, Murray GL, Adler B, Hendrixson DR, Buschiazzo A, Guo S, Liu J, Picardeau M. Role of the major determinant of polar flagellation FlhG in the endoflagella‐containing spirochete Leptospira. Molecular Microbiology 2021, 116: 1392-1406. PMID: 34657338, DOI: 10.1111/mmi.14831.Peer-Reviewed Original ResearchConceptsWild-type strainSaprophyte L. biflexaCross-species complementationComparative transcriptome analysisPathogen L. interrogansFlagellar basal bodyCryo-electron tomographySpirochete LeptospiraSpiral-shaped morphologyFlagellar genesFlhGNumerical regulationTranscriptome analysisPeriplasmic flagellaFlhFCell motilityNegative regulatorBasal bodiesBacterial speciesL. biflexaMutantsGel-like environmentL. interrogansFlagellaBacteriaBB0259 Encompasses a Peptidoglycan Lytic Enzyme Function for Proper Assembly of Periplasmic Flagella in Borrelia burgdorferi
Xu H, Hu B, Flesher DA, Liu J, Motaleb MA. BB0259 Encompasses a Peptidoglycan Lytic Enzyme Function for Proper Assembly of Periplasmic Flagella in Borrelia burgdorferi. Frontiers In Microbiology 2021, 12: 692707. PMID: 34659138, PMCID: PMC8517470, DOI: 10.3389/fmicb.2021.692707.Peer-Reviewed Original ResearchPeriplasmic flagellaFlagellar rodProper assemblyFlagellar hookCryo-electron tomographyPG sacculusProtein homologsΕ-ProteobacteriaPeptidoglycan sacculusLytic transglycosylaseΓ-ProteobacteriaDistinct proteinsFlgJOuter membraneFunctional flagellaFilament assemblyFunctional domainsEnzyme functionCell wallMutant strainLyme disease spirocheteFlagellaEnzyme activityAssemblySacculus
2020
A CRISPR Interference Platform for Selective Downregulation of Gene Expression in Borrelia burgdorferi
Takacs CN, Scott M, Chang Y, Kloos ZA, Irnov I, Rosa PA, Liu J, Jacobs-Wagner C. A CRISPR Interference Platform for Selective Downregulation of Gene Expression in Borrelia burgdorferi. Applied And Environmental Microbiology 2020, 87: e02519-20. PMID: 33257311, PMCID: PMC7851697, DOI: 10.1128/aem.02519-20.Peer-Reviewed Original ResearchCRISPR interference platformDifferent antibiotic resistance markersGene functionAntibiotic resistance markersGene expressionHomologous recombination-based methodsCell morphogenesis genesCell wall elongationNative expression levelsBasic cellular processesRecombination-based methodGene function studiesCryo-electron tomographyFuture genetic studiesMorphogenesis genesResistance markersRepression efficiencyCell straighteningGenetic toolsCellular processesWall elongationPeriplasmic flagellaCell filamentationCell divisionCellular motilityFlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi
Zhang K, He J, Catalano C, Guo Y, Liu J, Li C. FlhF regulates the number and configuration of periplasmic flagella in Borrelia burgdorferi. Molecular Microbiology 2020, 113: 1122-1139. PMID: 32039533, PMCID: PMC8085991, DOI: 10.1111/mmi.14482.Peer-Reviewed Original ResearchConceptsPeriplasmic flagellaCell polesM-ring proteinLyme disease bacterium Borrelia burgdorferiCryo-electron tomography studiesSignal recognition particlePolar localizationB. burgdorferiFlagellar assemblyRecognition particleMutant cellsFlagellar numberProtein stabilityFlagellar patternBorrelia burgdorferiFlhFEnzymatic activityBiochemical analysisMechanistic insightsBacterium Borrelia burgdorferiFlagellaPF numberBacteriaMidcellDetailed characterization
2019
Architecture and Assembly of Periplasmic Flagellum
Chang Y, Liu J. Architecture and Assembly of Periplasmic Flagellum. 2019, 189-199. DOI: 10.1128/9781683670285.ch16.Peer-Reviewed Original ResearchPeriplasmic flagellaVirulence of bacterial pathogensMotility of spirochetesAssociated with virulenceBacteria encounterAssemble flagellaPeritrichous flagellaFlagellar numberSalmonella entericaFlagellar structureCell polesVibrio sppPeriplasmic spaceOuter membraneBacterial pathogensBacterial speciesEscherichia coliFlagellaPseudomonas aeruginosaBacteriaMotilitySpeciesSpirochetesAssemblySalmonellaAnalysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi
Zhang K, Qin Z, Chang Y, Liu J, Malkowski MG, Shipa S, Li L, Qiu W, Zhang J, Li C. Analysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi. Molecular Microbiology 2019, 111: 1652-1670. PMID: 30883947, PMCID: PMC6561814, DOI: 10.1111/mmi.14243.Peer-Reviewed Original ResearchConceptsPeriplasmic flagellaFliD mutantFlagellin proteinMajor flagellin proteinLyme disease spirochete Borrelia burgdorferiFlagellar cap proteinFlagellar cap protein FliDFlagellar filament assemblyFlagella-deficient mutantsMutant cellsCAP mutantsFlaB proteinsPeriplasmFilament assemblyCap proteinB. burgdorferiFlagellar filamentsGenetic studiesMutantsBorrelia burgdorferiHtrASerine proteasesFliDFlagellin polymerizationSpirochete Borrelia burgdorferi
2018
Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex
Qin Z, Tu J, Lin T, Norris SJ, Li C, Motaleb MA, Liu J. Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex. PLOS Biology 2018, 16: e3000050. PMID: 30412577, PMCID: PMC6248999, DOI: 10.1371/journal.pbio.3000050.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyPeriplasmic flagellaATPase complexFlagellar C-ringType III secretion systemCytoplasmic ATPase complexLyme disease spirochete Borrelia burgdorferiMotility of spirochetesExport apparatusSecretion systemStructural insightsBorrelia burgdorferiFlagellaSpirochete Borrelia burgdorferiPathogenic spirochetesC-ringNovel therapeutic strategiesUnique mechanismDistinct morphologiesB. burgdorferiComplexesMultiple spokesAssemblyTherapeutic strategiesBurgdorferiThe Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum
Zhu S, Nishikino T, Kojima S, Homma M, Liu J. The Vibrio H-Ring Facilitates the Outer Membrane Penetration of the Polar Sheathed Flagellum. Journal Of Bacteriology 2018, 200: 10.1128/jb.00387-18. PMID: 30104237, PMCID: PMC6182240, DOI: 10.1128/jb.00387-18.Peer-Reviewed Original ResearchConceptsPolar sheathed flagellumPeriplasmic flagellaExternal flagellaOuter membraneSheathed flagellumBacterial life cycleCryo-electron tomographyWild-type cellsInternal periplasmic flagellaMultiple peritrichous flagellaRemarkable nanomachinesFlagellar genesPeritrichous flagellaPeriplasmic spaceMost bacteriaNovel functionMolecular basisBacterial flagellaMajor organellesBacterial speciesFlagellaMembrane penetrationH-ringGenesLife cycle
2016
A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete
Wunder EA, Figueira CP, Benaroudj N, Hu B, Tong BA, Trajtenberg F, Liu J, Reis MG, Charon NW, Buschiazzo A, Picardeau M, Ko AI. A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete. Molecular Microbiology 2016, 101: 457-470. PMID: 27113476, PMCID: PMC4979076, DOI: 10.1111/mmi.13403.Peer-Reviewed Original ResearchConceptsTraverse tissue barriersHamster modelTarget organsSystemic infectionClinical isolatesLeptospira spirochetesTranslational motilityL. interrogansCell morphologyTissue barriersMotilityLeptospiraPeriplasmic flagellaSpirochetesVirulence phenotypesProtein AHelical cell morphologyInfectionDiseaseLeptospirosisPathogen L. interrogans
2012
The Unique Paradigm of Spirochete Motility and Chemotaxis
Charon N, Cockburn A, Li C, Liu J, Miller K, Miller M, Motaleb M, Wolgemuth C. The Unique Paradigm of Spirochete Motility and Chemotaxis. Annual Review Of Microbiology 2012, 66: 349-370. PMID: 22994496, PMCID: PMC3771095, DOI: 10.1146/annurev-micro-092611-150145.Peer-Reviewed Original ResearchConceptsPeriplasmic flagellaSpirochete motilityIn situ analysis of cellsLyme disease spirochete Borrelia burgdorferiProtoplasmic cell cylinderGene regulationAnalysis of cellsOuter membraneUnique bacteriaCell cylinderExternal appendagesCryoelectron tomographyFlagellated bacteriaMotilitySpirochete Borrelia burgdorferiBacteriaChemotaxisModel systemLife cycleSpirochetesFlagellaCellsBacteriumGenesTranslocation
1995
The hook protein of Borrelia burgdorferi, encoded by the flgE gene, is serologically recognized in Lyme disease.
Jwang B, Dewing P, Fikrig E, Flavell RA. The hook protein of Borrelia burgdorferi, encoded by the flgE gene, is serologically recognized in Lyme disease. MSphere 1995, 2: 609-15. PMID: 8548542, PMCID: PMC170207, DOI: 10.1128/cdli.2.5.609-615.1995.Peer-Reviewed Original ResearchConceptsFlgE proteinFlgE geneEscherichia coli expression plasmidPrimary protein sequenceB. burgdorferi N40Hook geneWhole cell lysatesHook proteinLinear chromosomesPeriplasmic flagellaProtein sequencesFlgERecombinant proteinsB. burgdorferiBasal bodiesFlagellar filamentsWestern blot analysisBorrelia burgdorferiGenesExpression plasmidProteinBlot analysisNegative bacteriaMurine antiseraLyme disease
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