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 tissue
2020
Molecular mechanism for rotational switching of the bacterial flagellar motor
Chang Y, Zhang K, Carroll BL, Zhao X, Charon NW, Norris SJ, Motaleb MA, Li C, Liu J. Molecular mechanism for rotational switching of the bacterial flagellar motor. Nature Structural & Molecular Biology 2020, 27: 1041-1047. PMID: 32895555, PMCID: PMC8129871, DOI: 10.1038/s41594-020-0497-2.Peer-Reviewed Original ResearchConceptsBacterial flagellar motorSwitch proteinFlagellar motorResponse regulator CheYRotational switchingProton motive forceSwitch complexMolecular mechanismsPhosphorylated formMajor remodelingConformational changesMotive forceModel systemProteinBorrelia burgdorferiCheY3CheYMutantsTorque generatorFLIMInteractsCheXCW rotationMechanismRemodelingFlhF 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
Analysis 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 strategiesBurgdorferi
2017
In Situ Structural Analysis of the Spirochetal Flagellar Motor by Cryo-Electron Tomography
Zhu S, Qin Z, Wang J, Morado DR, Liu J. In Situ Structural Analysis of the Spirochetal Flagellar Motor by Cryo-Electron Tomography. Methods In Molecular Biology 2017, 1593: 229-242. PMID: 28389958, DOI: 10.1007/978-1-4939-6927-2_18.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyFlagellar motorIntact flagellar motorBacterial flagellar motorMolecular machinerySitu structural analysisExtensive structural analysisMolecular machinesLarge complexesStructural analysisUnprecedented detailBorrelia burgdorferiStructural determinationMachineryOrganismsBacteriaPowerful techniqueCellsComplexesBurgdorferi