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
2024
PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa
Guo S, Chang Y, Brun Y, Howell P, Burrows L, Liu J. PilY1 regulates the dynamic architecture of the type IV pilus machine in Pseudomonas aeruginosa. Nature Communications 2024, 15: 9382. PMID: 39477930, PMCID: PMC11525922, DOI: 10.1038/s41467-024-53638-y.Peer-Reviewed Original ResearchConceptsPilus extensionCell envelopeType IV piliPathogen Pseudomonas aeruginosaBacterial cell envelopeP. aeruginosa cellsCryo-electron tomographyPilus dynamicsPilin subunitSecretin channelSurface motilityPriming complexOuter membraneBiofilm formationT4PPilY1P. aeruginosaPseudomonas aeruginosaCentral poreMolecular mechanismsSubtomogram averagingPotential therapeutic targetDynamic assemblyTherapeutic targetMolecular framework
2023
Cryo-electron tomography of intact cardiac muscle reveals myosin binding protein-C linking myosin and actin filaments
Huang X, Torre I, Chiappi M, Yin Z, Vydyanath A, Cao S, Raschdorf O, Beeby M, Quigley B, de Tombe P, Liu J, Morris E, Luther P. Cryo-electron tomography of intact cardiac muscle reveals myosin binding protein-C linking myosin and actin filaments. Journal Of Muscle Research And Cell Motility 2023, 44: 165-178. PMID: 37115473, PMCID: PMC10542292, DOI: 10.1007/s10974-023-09647-3.Peer-Reviewed Original ResearchConceptsMyBP-CMyosin-binding protein CCryo-electron tomographyStripes 4Binding protein CRod-shaped proteinN-terminal domainC-terminal regionCardiac MyBP-CActin filamentsAccessory proteinsCentral domainMyosin headsSubtomogram averagingActinMyosinTokuyasu cryosectionsProtein CCardiac muscleFilamentsProteinStripesC-zoneDependent fashionA-band
2022
In situ architecture of the lipid transport protein VPS13C at ERâlysosome membrane contacts
Cai S, Wu Y, GuillĂ©n-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. In situ architecture of the lipid transport protein VPS13C at ERâlysosome membrane contacts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203769119. PMID: 35858323, PMCID: PMC9303930, DOI: 10.1073/pnas.2203769119.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCryo-focused ion beam millingMembrane contact sitesCryo-electron tomographyFull-length structureLipid transport proteinsRod-like densitiesLysosome contactBinding partnerGenetic approachesHydrophobic grooveTransport proteinsContact sitesVps13Lipid transportAlphaFold predictionsFull-length modelHeLa cellsMembrane contactSitu architectureAdjacent membranesVPS13CProteinStructural informationEndo/lysosomesFliL 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 fluxProteinFunctionAssemblyRemodelingCellsConformationBorreliaIn-situ high-resolution 3D imaging combined with proteomics and metabolomics reveals enlargement of subcellular architecture and enhancement of photosynthesis pathways in nuclear-irradiated Chlorella pyrenoidosa
Guo W, Feng L, Wang Z, Guo J, Park D, Carroll B, Zhang X, Liu J, Cheng J. In-situ high-resolution 3D imaging combined with proteomics and metabolomics reveals enlargement of subcellular architecture and enhancement of photosynthesis pathways in nuclear-irradiated Chlorella pyrenoidosa. Chemical Engineering Journal 2022, 430: 133037. DOI: 10.1016/j.cej.2021.133037.Peer-Reviewed Original ResearchPhotosynthetic efficiencySubcellular organellesChlorella pyrenoidosaHigh growth rateCryo-electron tomographyWild-type cellsPhotosynthesis pathwaySubcellular architectureCarbon fixationCryo-FIB millingChlorophyll synthesisMutantsGrowth rateMacroscopic traitsOrganellesSubcellular morphologyC. pyrenoidosaProteomicsBeam scanning electron microscopyIon beam scanning electron microscopyMetabolomics dataPyrenoidosaUnprecedented detailSuch modificationsChloroplasts
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 endoflagellaâcontaining spirochete Leptospira
Fule L, Halifa R, Fontana C, Sismeiro O, Legendre R, Varet H, CoppĂ©e 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 endoflagellaâcontaining 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 homologsÎ-ProteobacteriaPeptidoglycan sacculusLytic transglycosylaseÎ-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 motilityThe flagellar motor of Vibrio alginolyticus undergoes major structural remodeling during rotational switching
Carroll BL, Nishikino T, Guo W, Zhu S, Kojima S, Homma M, Liu J. The flagellar motor of Vibrio alginolyticus undergoes major structural remodeling during rotational switching. ELife 2020, 9: e61446. PMID: 32893817, PMCID: PMC7505661, DOI: 10.7554/elife.61446.Peer-Reviewed Original ResearchConceptsFlagellar motorRotational switchingBacterial flagellar motorLarge conformational rearrangementsCryo-electron tomographyMajor structural remodelingConformational remodelingRotor complexCytoplasmic ringConformational rearrangementsProtein compositionConformational changesC-ringNovel insightsFliNFlagellaMolecular architectureFLIMVibrioFliGRemodelingMutantsStructural remodelingMechanismCellsMBIR 3D Reconstruction Method Effectively Minimizes Missing Wedge Artifacts and Restores Missing Information in Cryo-electron Tomography
Yan R, Venkatakrishnan S, Liu J, Bouman C, Jiang W. MBIR 3D Reconstruction Method Effectively Minimizes Missing Wedge Artifacts and Restores Missing Information in Cryo-electron Tomography. Microscopy And Microanalysis 2020, 26: 3146-3149. DOI: 10.1017/s143192762002396x.Peer-Reviewed Original ResearchMissing wedge artifactsCryo-electron tomographyWedge artifactsCryo-electronMBIRRestore missing informationAn 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 meansEndoflagellaApplying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System.
Chetrit D, Park D, Hu B, Liu J, Roy CR. Applying Live Cell Imaging and Cryo-Electron Tomography to Resolve Spatiotemporal Features of the Legionella pneumophila Dot/Icm Secretion System. Journal Of Visualized Experiments 2020 PMID: 32225141, DOI: 10.3791/60693.Peer-Reviewed Original ResearchConceptsDot/Icm secretion systemCryo-electron tomographySecretion systemCryo-ETDot/Icm systemDot/Icm apparatusDot/IcmSuperfolder green fluorescent proteinLive-cell imagingGreen fluorescent proteinIntact bacterial cellsPolar positioningSecretion complexPolar localizationQuantitative fluorescence microscopyBacterial poleATPase geneCytoplasmic complexDelivery of proteinsDNA substratesTiming of productionIcm systemFluorescent proteinLiving cellsBacterial cellsIn Situ Structure of the Vibrio Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator
Zhu S, Nishikino T, Takekawa N, Terashima H, Kojima S, Imada K, Homma M, Liu J. In Situ Structure of the Vibrio Polar Flagellum Reveals a Distinct Outer Membrane Complex and Its Specific Interaction with the Stator. Journal Of Bacteriology 2020, 202: 10.1128/jb.00592-19. PMID: 31767780, PMCID: PMC6989802, DOI: 10.1128/jb.00592-19.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsCryo-electron tomographyStator unitsFlagellar rotationDetailed protein-protein interactionsUnique protein-protein interactionsGram-negative marine bacteriumPolar sheathed flagellumBasal body structureHigh-speed motilityBacterial flagellar motorLarge conformational changesSpecific interactionsFirst structural evidencePeriplasmic domainPolar flagellumFlagellar motorPeptidoglycan layerMembrane complexT ringMarine bacteriumBacterial flagellaGenetic analysisDetailed structural informationSheathed flagellum
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, GalĂĄn 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 variationStructural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography
Wang C, Tu J, Liu J, Molineux IJ. Structural dynamics of bacteriophage P22 infection initiation revealed by cryo-electron tomography. Nature Microbiology 2019, 4: 1049-1056. PMID: 30886360, PMCID: PMC6533119, DOI: 10.1038/s41564-019-0403-z.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyOuter membraneInfection initiationCell surfaceBacterial cell envelopeSalmonella enterica serovar TyphimuriumGenome translocationGram-negative bacteriaEnterica serovar TyphimuriumTail needleCytoplasmic membraneSecond proteinExtracellular channelsCell envelopePhage P22Successful infectionCell cytoplasmSerovar TyphimuriumSuch virionsGenomeCytoplasmProteinO-antigenPhagesAssembles
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
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