2024
Bacterial flagella hijack type IV pili proteins to control motility
Liu X, Tachiyama S, Zhou X, Mathias R, Bonny S, Khan M, Xin Y, Roujeinikova A, Liu J, Ottemann K. Bacterial flagella hijack type IV pili proteins to control motility. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2317452121. PMID: 38236729, PMCID: PMC10823254, DOI: 10.1073/pnas.2317452121.Peer-Reviewed Original Research
2022
A Tripartite Efflux System Affects Flagellum Stability in Helicobacter pylori
Gibson K, Chu JK, Zhu S, Nguyen D, Mrázek J, Liu J, Hoover TR. A Tripartite Efflux System Affects Flagellum Stability in Helicobacter pylori. International Journal Of Molecular Sciences 2022, 23: 11609. PMID: 36232924, PMCID: PMC9570263, DOI: 10.3390/ijms231911609.Peer-Reviewed Original ResearchConceptsTripartite efflux systemEfflux systemPeriplasmic membrane fusion proteinOuter membrane efflux proteinCryo-electron tomography studiesMembrane efflux proteinMembrane fusion proteinNumber of flagellaTransmembrane domainABC transportersUnsheathed flagellaSwimming motilityCandidate proteinsFusion proteinEfflux proteinsSame frameshift mutationFlagellaEnhanced motilityMutantsFlagellar sheathFrameshift mutationProteinIndependent variantsHomologP ringFliL 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
An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete
Gibson KH, Trajtenberg F, Wunder EA, Brady MR, San Martin F, Mechaly A, Shang Z, Liu J, Picardeau M, Ko A, Buschiazzo A, Sindelar CV. An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete. ELife 2020, 9: e53672. PMID: 32157997, PMCID: PMC7065911, DOI: 10.7554/elife.53672.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyKey functional attributesNative flagellar filamentsHigh-resolution cryo-electron tomographyPeriplasmic spaceSheath proteinStructural basisFlagellar filamentsLeptospira spirochetesSpirochete bacteriaEntire cellFunctional attributesX-ray crystallographyImportant pathogenSupercoilingMotilityBacteriaFilamentsCell bodiesFlagellaSpirochetesProteinFlagellinDistinctive meansEndoflagellaFlhF 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
Loss of a Cardiolipin Synthase in Helicobacter pylori G27 Blocks Flagellum Assembly
Chu JK, Zhu S, Herrera CM, Henderson JC, Liu J, Trent MS, Hoover TR. Loss of a Cardiolipin Synthase in Helicobacter pylori G27 Blocks Flagellum Assembly. Journal Of Bacteriology 2019, 201: 10.1128/jb.00372-19. PMID: 31427391, PMCID: PMC6779456, DOI: 10.1128/jb.00372-19.Peer-Reviewed Original ResearchConceptsFlagellum assemblyFlagellum biosynthesisCardiolipin synthaseFlagellar protein export apparatusCardiolipin levelsProtein export apparatusCryo-electron tomographyWild-type levelsAllelic exchange mutagenesisMS ringFlagellar genesExport apparatusCell polesP ringHost colonizationMature flagellumCell envelopeGenomic DNAMutantsProximal rodFlagellaBiosynthesisSequencing analysisFlgIBacterial pathogensIn Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography
Zhu S, Schniederberend M, Zhitnitsky D, Jain R, Galán JE, Kazmierczak BI, Liu J. In Situ Structures of Polar and Lateral Flagella Revealed by Cryo-Electron Tomography. Journal Of Bacteriology 2019, 201: 10.1128/jb.00117-19. PMID: 31010901, PMCID: PMC6560136, DOI: 10.1128/jb.00117-19.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyBacterial flagellaFlagellar assemblyPolar flagellumPeritrichous flagellaSerovar TyphimuriumSpecies-specific featuresBacterial pathogensOuter membrane complexSelf-assembling nanomachineFlagellar systemFlagellar structureFlagellar numberSubtomogram averagingMembrane complexLateral flagellaStructural basisDistinct flagellaMolecular machinesFlagellaSitu structureModel systemPseudomonasTyphimuriumRange of variation
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
2017
Molecular architecture of the sheathed polar flagellum in Vibrio alginolyticus
Zhu S, Nishikino T, Hu B, Kojima S, Homma M, Liu J. Molecular architecture of the sheathed polar flagellum in Vibrio alginolyticus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 10966-10971. PMID: 28973904, PMCID: PMC5642721, DOI: 10.1073/pnas.1712489114.Peer-Reviewed Original ResearchConceptsPolar flagellumOuter membraneIntact cellsFlagellar motor componentsSheathed polar flagellumRod-shaped bacteriaGram-negative rod-shaped bacteriaLimited structural informationPeriplasmic structureSubtomogram analysisFlagellar rotationFlagellar motorGenetic approachesUnsheathed flagellaCryoelectron tomographySwimming motilitySheathed flagellumMajor remodelingFlagellaRing-like structureMolecular levelDistinct motilityFast motilityMembranous sheathLength variation
2016
Imaging the Motility and Chemotaxis Machineries in Helicobacter pylori by Cryo-Electron Tomography
Qin Z, Lin WT, Zhu S, Franco AT, Liu J. Imaging the Motility and Chemotaxis Machineries in Helicobacter pylori by Cryo-Electron Tomography. Journal Of Bacteriology 2016, 199: 10.1128/jb.00695-16. PMID: 27849173, PMCID: PMC5237115, DOI: 10.1128/jb.00695-16.Peer-Reviewed Original ResearchCryo-electron tomographyChemotaxis arraysUnipolar flagellaBacterial pathogensFlagella-driven motilityMultiple unipolar flagellaNovel structural insightsFlagellar assemblyChemotaxis machineryFlagellar poleAssembly intermediatesFlagellar rotationFlagellar motorCell envelopeStructural insightsMembrane sheathSheathed flagellumMolecular mechanismsUnique motilityH. pylori cellsFlagellaSitu structureHigh-viscosity environmentsPylori cellsMotility