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
2023
Bacteria require phase separation for fitness in the mammalian gut
Krypotou E, Townsend G, Gao X, Tachiyama S, Liu J, Pokorzynski N, Goodman A, Groisman E. Bacteria require phase separation for fitness in the mammalian gut. Science 2023, 379: 1149-1156. PMID: 36927025, PMCID: PMC10148683, DOI: 10.1126/science.abn7229.Peer-Reviewed Original ResearchConceptsMammalian gutTranscription termination factor RhoTermination factor RhoGene regulationTranscription terminationMechanisms bacteriaBacteria interactionsHuman commensalValuable targetBacteriaRhoGut microbiotaFitnessNovel clinical applicationsTherapeutic manipulationGutHuman healthCommensalRegulation
2022
Developmental Transitions Coordinate Assembly of the Coxiella burnetii Dot/Icm Type IV Secretion System
Park D, Steiner S, Shao M, Roy CR, Liu J. Developmental Transitions Coordinate Assembly of the Coxiella burnetii Dot/Icm Type IV Secretion System. Infection And Immunity 2022, 90: e00410-22. PMID: 36190257, PMCID: PMC9584302, DOI: 10.1128/iai.00410-22.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCoxiella burnetiiHost-Pathogen InteractionsLysosomesType IV Secretion SystemsVacuolesConceptsSmall cell variantLarge cell variantDot/Icm type IV secretion systemCell variantIntracellular replicationActive large cell variantHost cellsIntracellular bacterial pathogenType IV secretion systemDot/Icm T4SSObligate intracellular bacterial pathogenC. burnetiiCoxiella burnetiiBiphasic developmental cycleUnique biphasic developmental cycleInfectionNew host cellsSecretion systemBacterial pathogensInfectious formHost vacuoleBurnetiiMorphological changesCellsLater stagesA 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 ResearchMeSH KeywordsATP-Binding Cassette TransportersBacterial ProteinsFlagellaHelicobacter pyloriMembrane Fusion ProteinsMembrane ProteinsConceptsTripartite 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 ringIdentification 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. interrogansFlagellaBacteriaComposition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System
Tachiyama S, Skaar R, Chang Y, Carroll BL, Muthuramalingam M, Whittier SK, Barta ML, Picking WL, Liu J, Picking WD. Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System. Frontiers In Cellular And Infection Microbiology 2021, 11: 682635. PMID: 34150677, PMCID: PMC8211105, DOI: 10.3389/fcimb.2021.682635.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesBacterial ProteinsProtein TransportShigellaShigella flexneriType III Secretion SystemsConceptsType III secretion systemCytoplasmic sorting platformSorting platformSecretion systemTwo-hybrid analysisCryo-electron tomography dataC-terminal domainShigella type III secretion systemFull-length copiesBiophysical propertiesDistinct biophysical propertiesSpa47 ATPaseT3SS injectisomeEffector proteinsSecretion substratesDistinct complexesIntracellular nicheBasal bodiesPrimary virulence factorSpa33Host cellsHeterotrimerPrecise makeupVirulence factorsMxiKThe peptidoglycan-associated protein NapA plays an important role in the envelope integrity and in the pathogenesis of the lyme disease spirochete
Davis MM, Brock AM, DeHart TG, Boribong BP, Lee K, McClune ME, Chang Y, Cramer N, Liu J, Jones CN, Jutras BL. The peptidoglycan-associated protein NapA plays an important role in the envelope integrity and in the pathogenesis of the lyme disease spirochete. PLOS Pathogens 2021, 17: e1009546. PMID: 33984073, PMCID: PMC8118282, DOI: 10.1371/journal.ppat.1009546.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBorrelia burgdorferiCell WallChemokines, CXCHumansLyme DiseasePeptidoglycanConceptsPeptidoglycan-associated proteinsCell envelopeUnbiased proteomic approachCryo-electron microscopyOxidative stress responseOuter membrane vesiclesGram-negative bacteriaDps homologueEnvelope integrityProteomic approachNapA mutantOuter membraneBacterial proteinsMutant bacteriaDNA bindingCritical residuesBiological functionsLyme disease spirocheteStress responseCellular DNAMembrane vesiclesPeptidoglycanEnvelope layersBacterial pathogensCellular studies
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 rotationMechanismRemodelingEstablishing rod shape from spherical, peptidoglycan-deficient bacterial spores
Zhang H, Mulholland GA, Seef S, Zhu S, Liu J, Mignot T, Nan B. Establishing rod shape from spherical, peptidoglycan-deficient bacterial spores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 14444-14452. PMID: 32513721, PMCID: PMC7321990, DOI: 10.1073/pnas.2001384117.Peer-Reviewed Original ResearchConceptsBacterial actin homolog MreBFuture cell polesActin homolog MreBGTPase-activating proteinsMolecular motorsGram-negative bacteriumCell polesEukaryotic cellsSynthesis complexSpherical sporesWalled cellsRod shapeMglBMglAPG growthSporesMreBBacterial sporesGTPaseCellsCytoskeletonMyxococcusPeptidoglycanProteinBacteriumAn 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 cellsFlhF 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 ResearchMeSH KeywordsBacterial ProteinsBasal BodiesBorrelia burgdorferiElectron Microscope TomographyFlagellaGene DeletionLocomotionMonomeric GTP-Binding ProteinsConceptsPeriplasmic 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 characterizationAnalysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding
Park D, Chetrit D, Hu B, Roy CR, Liu J. Analysis of Dot/Icm Type IVB Secretion System Subassemblies by Cryoelectron Tomography Reveals Conformational Changes Induced by DotB Binding. MBio 2020, 11: 10.1128/mbio.03328-19. PMID: 32071271, PMCID: PMC7029142, DOI: 10.1128/mbio.03328-19.Peer-Reviewed Original ResearchConceptsType IV secretion systemSecretion systemCryoelectron tomographyInner membraneDot/Icm apparatusConformational changesDot/IcmEukaryotic host cellsBacterial inner membraneWild-type cellsHost cell membraneWhole-cell contextMultiprotein nanomachineSubtomogram analysisSophisticated nanomachinesCytoplasmic substratesProtein effectorsCell polesDNA substratesSubtomogram averagingATPase complexDNA transferHost infectionStructural basisHost 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
High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway
Butan C, Lara-Tejero M, Li W, Liu J, Galán JE. High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 24786-24795. PMID: 31744874, PMCID: PMC6900529, DOI: 10.1073/pnas.1916331116.Peer-Reviewed Original ResearchThe cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the Shigella type III secretion system
Tachiyama S, Chang Y, Muthuramalingam M, Hu B, Barta ML, Picking WL, Liu J, Picking WD. The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the Shigella type III secretion system. Journal Of Biological Chemistry 2019, 294: 19184-19196. PMID: 31699894, PMCID: PMC6916477, DOI: 10.1074/jbc.ra119.009125.Peer-Reviewed Original ResearchConceptsInner membrane ringType III secretion systemCytoplasmic domainSecretion systemCytoplasmic sorting platformForkhead-associated (FHA) domainShigella type III secretion systemDiverse bacterial pathogensDisruption of interactionsSpa47 ATPaseStructure-function relationshipsExtracellular needleEffector recognitionGram-negative bacteriaEukaryotic cellsT3SS apparatusVirulence effectorsMembrane ringSorting platformInsertional mutagenesisGenetic methodsHomologous interactionsMxiKTip complexBasal bodiesLoss 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 pathogens