2020
Subnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles
Li Z, Li W, Lu M, Bess J, Chao CW, Gorman J, Terry DS, Zhang B, Zhou T, Blanchard SC, Kwong PD, Lifson JD, Mothes W, Liu J. Subnanometer structures of HIV-1 envelope trimers on aldrithiol-2-inactivated virus particles. Nature Structural & Molecular Biology 2020, 27: 726-734. PMID: 32601441, PMCID: PMC8138683, DOI: 10.1038/s41594-020-0452-2.Peer-Reviewed Original ResearchApplying 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 ResearchMeSH KeywordsAdenosine TriphosphatasesBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyLegionella pneumophilaModels, MolecularProtein ConformationType IV Secretion SystemsConceptsType 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 ResearchMeSH KeywordsBacterial Outer Membrane ProteinsBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyFlagellaMolecular Motor ProteinsProtein ConformationVibrio alginolyticusConceptsProtein-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
In 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 ResearchMeSH KeywordsBacterial ProteinsCryoelectron MicroscopyElectron Microscope TomographyFlagellaGene Expression Regulation, BacterialPseudomonas aeruginosaSalmonella typhimuriumConceptsCryo-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 ResearchMeSH KeywordsAdenosine TriphosphatasesBacterial ProteinsBorrelia burgdorferiCytoplasmElectron Microscope TomographyFlagellaPeriplasmType III Secretion SystemsConceptsCryo-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 strategiesBurgdorferiVisualization of the type III secretion mediated Salmonella–host cell interface using cryo-electron tomography
Park D, Lara-Tejero M, Waxham MN, Li W, Hu B, Galán JE, Liu J. Visualization of the type III secretion mediated Salmonella–host cell interface using cryo-electron tomography. ELife 2018, 7: e39514. PMID: 30281019, PMCID: PMC6175578, DOI: 10.7554/elife.39514.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCell MembraneElectron Microscope TomographyHeLa CellsHost-Pathogen InteractionsHumansMutationProtein TransportSalmonella typhimuriumType III Secretion SystemsConceptsCryo-electron tomographyEffector translocationBacterial-host cell contactType III protein secretion systemProtein secretion systemHost cell interfaceProtein secretion machinesCell membraneComplex host-pathogen interactionsType III secretionHost-pathogen interactionsHost cell membraneTarget cell membraneNegative bacterial pathogensTranslocon poreSecretion machineEffector proteinsSecretion systemHost cellsBacterial pathogensCell contactCell interfaceIntimate associationTranslocationBacteriaVisualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis
Qin Z, Hu B, Liu J. Visualizing Chemoreceptor Arrays in Bacterial Minicells by Cryo-Electron Tomography and Subtomogram Analysis. Methods In Molecular Biology 2018, 1729: 187-199. PMID: 29429093, DOI: 10.1007/978-1-4939-7577-8_17.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsChemotactic FactorsChemotaxisCryoelectron MicroscopyElectron Microscope TomographyHistidine KinaseSalmonella entericaSignal TransductionConceptsCryo-electron tomographyChemoreceptor arraysCheW coupling proteinLarge macromolecular assembliesChemotaxis arraysSubtomogram analysisCheA kinaseBacterial chemoreceptorsCellular contextCoupling proteinMacromolecular assembliesChemotaxis signalingMolecular levelSitu structurePrecise architectureBacterial minicellsMinicellsUnique toolKinaseSignalingProteinSubtomogramsAssemblyConcertAmplification
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 variationIn 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 ResearchMeSH KeywordsBacterial ProteinsBorrelia burgdorferiCryoelectron MicroscopyElectron Microscope TomographyFlagellaMolecular Motor ProteinsConceptsCryo-electron tomographyFlagellar motorIntact flagellar motorBacterial flagellar motorMolecular machinerySitu structural analysisExtensive structural analysisMolecular machinesLarge complexesStructural analysisUnprecedented detailBorrelia burgdorferiStructural determinationMachineryOrganismsBacteriaPowerful techniqueCellsComplexesBurgdorferi
2011
Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle
Luther PK, Winkler H, Taylor K, Zoghbi ME, Craig R, Padrón R, Squire JM, Liu J. Direct visualization of myosin-binding protein C bridging myosin and actin filaments in intact muscle. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 11423-11428. PMID: 21705660, PMCID: PMC3136262, DOI: 10.1073/pnas.1103216108.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBiophysical PhenomenaCarrier ProteinsElectron Microscope TomographyFreeze SubstitutionHumansImaging, Three-DimensionalModels, MolecularMuscle, SkeletalMyosinsRanidae
2010
Electron Tomography of Cryofixed, Isometrically Contracting Insect Flight Muscle Reveals Novel Actin-Myosin Interactions
Wu S, Liu J, Reedy MC, Tregear RT, Winkler H, Franzini-Armstrong C, Sasaki H, Lucaveche C, Goldman YE, Reedy MK, Taylor KA. Electron Tomography of Cryofixed, Isometrically Contracting Insect Flight Muscle Reveals Novel Actin-Myosin Interactions. PLOS ONE 2010, 5: e12643. PMID: 20844746, PMCID: PMC2936580, DOI: 10.1371/journal.pone.0012643.Peer-Reviewed Original Research
2009
Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle
Wu S, Liu J, Reedy MC, Winkler H, Reedy MK, Taylor KA. Methods for identifying and averaging variable molecular conformations in tomograms of actively contracting insect flight muscle. Journal Of Structural Biology 2009, 168: 485-502. PMID: 19698791, PMCID: PMC2805068, DOI: 10.1016/j.jsb.2009.08.007.Peer-Reviewed Original Research
2008
Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes
Winkler H, Zhu P, Liu J, Ye F, Roux KH, Taylor KA. Tomographic subvolume alignment and subvolume classification applied to myosin V and SIV envelope spikes. Journal Of Structural Biology 2008, 165: 64-77. PMID: 19032983, PMCID: PMC2656979, DOI: 10.1016/j.jsb.2008.10.004.Peer-Reviewed Original Research