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 ResearchMeSH KeywordsCryoelectron MicroscopyElectron Microscope TomographyFimbriae ProteinsFimbriae, BacterialModels, MolecularPseudomonas aeruginosaConceptsPilus 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 frameworkStructure and inhibition of SARS-CoV-2 spike refolding in membranes
Grunst M, Qin Z, Dodero-Rojas E, Ding S, Prévost J, Chen Y, Hu Y, Pazgier M, Wu S, Xie X, Finzi A, Onuchic J, Whitford P, Mothes W, Li W. Structure and inhibition of SARS-CoV-2 spike refolding in membranes. Science 2024, 385: 757-765. PMID: 39146425, PMCID: PMC11449073, DOI: 10.1126/science.adn5658.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralBetacoronavirusCell MembraneCOVID-19Cryoelectron MicroscopyElectron Microscope TomographyHumansMolecular Dynamics SimulationPeptidyl-Dipeptidase AProtein DomainsProtein MultimerizationProtein RefoldingSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationNative architecture of a human GBP1 defense complex for cell-autonomous immunity to infection
Zhu S, Bradfield C, Maminska A, Park E, Kim B, Kumar P, Huang S, Kim M, Zhang Y, Bewersdorf J, MacMicking J. Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection. Science 2024, 383: eabm9903. PMID: 38422126, DOI: 10.1126/science.abm9903.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4Surface of Gram-negative bacteriaGuanosine triphosphate hydrolysisImmunity to infectionInnate immunity to infectionCryo-electron tomographyGram-negative bacteriaImmunity proteinSignaling platformsMembrane insertionHuman cellsNative structureCombat infectionsLipopolysaccharide releaseGasdermin DExtended conformationLiving organismsProteinDefense complexCellsNative architectureGBP1BacteriaInfection
2023
HIV-1 Env trimers asymmetrically engage CD4 receptors in membranes
Li W, Qin Z, Nand E, Grunst M, Grover J, Bess J, Lifson J, Zwick M, Tagare H, Uchil P, Mothes W. HIV-1 Env trimers asymmetrically engage CD4 receptors in membranes. Nature 2023, 623: 1026-1033. PMID: 37993716, PMCID: PMC10686830, DOI: 10.1038/s41586-023-06762-6.Peer-Reviewed Original ResearchMeSH KeywordsAIDS VaccinesCapsidCD4 AntigensCell MembraneCryoelectron MicroscopyElectron Microscope TomographyHIV AntibodiesHIV Envelope Protein gp120HIV InfectionsHIV-1HumansProtein MultimerizationVirionConceptsHIV-1 Env trimersCD4 moleculeHuman immunodeficiency virus-1 (HIV-1) infectionEnv trimersAntibody-mediated immune responsesEnv-CD4 interactionVirus-1 infectionVaccine immunogen designViral envelope glycoproteinsHIV-1Immune responseCD4 receptorImmunogen designEnvelope glycoproteinVirus-like particlesCD4EnvHost cell membraneClostridioides difficile ferrosome organelles combat nutritional immunity
Pi H, Sun R, McBride J, Kruse A, Gibson-Corley K, Krystofiak E, Nicholson M, Spraggins J, Zhou Q, Skaar E. Clostridioides difficile ferrosome organelles combat nutritional immunity. Nature 2023, 623: 1009-1016. PMID: 37968387, PMCID: PMC10822667, DOI: 10.1038/s41586-023-06719-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell MembraneClostridioides difficileClostridium InfectionsCryoelectron MicroscopyDisease Models, AnimalElectron Microscope TomographyFerric CompoundsHomeostasisHost Microbial InteractionsInflammationIntestinesIronLeukocyte L1 Antigen ComplexMiceMicrobial ViabilityOrganellesConceptsFerric uptake regulator FurCryo-electron tomographyRegulator FurGram-negative bacteriaMembrane proteinsNutritional immunityIron uptakeCellular membranesDetoxification strategiesIron homeostasisForms of lifeStore ironBacterial pathogensIron sequestrationBiomineralization processPhosphate biomineralsRecent studiesImportant roleBacterial colonizationOrganellesInflamed gutMouse modelProteinTransportersHomeostasisCryo-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 ResearchMeSH KeywordsActin CytoskeletonActinsAnimalsElectron Microscope TomographyMammalsMyocardiumMyosinsRatsConceptsMyBP-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-bandNew frontier of cryo-electron microscopy technology
Sun F, Zhang X, Zhang K. New frontier of cryo-electron microscopy technology. Journal Of Molecular Biology 2023, 435: 168098. PMID: 37061087, DOI: 10.1016/j.jmb.2023.168098.Peer-Reviewed Original ResearchDetermining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA
Cheng J, Liu T, You X, Zhang F, Sui S, Wan X, Zhang X. Determining protein structures in cellular lamella at pseudo-atomic resolution by GisSPA. Nature Communications 2023, 14: 1282. PMID: 36922493, PMCID: PMC10017804, DOI: 10.1038/s41467-023-36175-y.Peer-Reviewed Original ResearchMeSH KeywordsCryoelectron MicroscopyElectron Microscope TomographyImage Processing, Computer-AssistedConceptsProtein complexesCellular lamellaTarget protein complexesCryo-electron tomographyProtein structure determinationCryo-electron microscopy imagesHigh-throughput data collectionProtein structureAtomic resolutionStructure determinationComplexesPhycobilisomesComplex structureMajor toolLamellaeHigh-resolution reconstruction
2022
Cryo-EM structures of prefusion SIV envelope trimer
Gorman J, Wang C, Mason R, Nazzari A, Welles H, Zhou T, Bess J, Bylund T, Lee M, Tsybovsky Y, Verardi R, Wang S, Yang Y, Zhang B, Rawi R, Keele B, Lifson J, Liu J, Roederer M, Kwong P. Cryo-EM structures of prefusion SIV envelope trimer. Nature Structural & Molecular Biology 2022, 29: 1080-1091. PMID: 36344847, PMCID: PMC10606957, DOI: 10.1038/s41594-022-00852-1.Peer-Reviewed Original Research
2021
Studying bacterial chemosensory array with CryoEM
Qin Z, Zhang P. Studying bacterial chemosensory array with CryoEM. Biochemical Society Transactions 2021, 49: 2081-2089. PMID: 34495335, PMCID: PMC8589424, DOI: 10.1042/bst20210080.Peer-Reviewed Original ResearchConceptsChemosensory arraysBacterial chemosensory arrayThousands of proteinsGradients of nutrientsCell polesLipid nanodiscsChemosensory systemCryoEMBacterial minicellsStructural studiesBacteria cellsBacterial ghostsRecent advancesMinicellsStructural analysisNanodiscsProteinBacteriaNutrientsCellsVivoStructural insights into the cause of human RSPH4A primary ciliary dyskinesia
Zhao Y, Pinskey J, Lin J, Yin W, Sears P, Daniels L, Zariwala M, Knowles M, Ostrowski L, Nicastro D. Structural insights into the cause of human RSPH4A primary ciliary dyskinesia. Molecular Biology Of The Cell 2021, 32: 1202-1209. PMID: 33852348, PMCID: PMC8351563, DOI: 10.1091/mbc.e20-12-0806.Peer-Reviewed Original ResearchMeSH KeywordsAxonemeCiliaCiliary Motility DisordersCytoskeletal ProteinsElectron Microscope TomographyHumansMutationRespiratory SystemConceptsStructural basisCryo-electron tomographyRadial spokesCentral pair complexUnderlying structural basisAxonemal repeatEukaryotic organellesArch domainThree-dimensional structureSubtomogram averagingOrgan positioningCell motilityStructural insightsPrimary ciliary dyskinesiaCiliaHuman ciliaHuman respiratory ciliaRS1Primary defectStructure determinationCiliary dyskinesiaHuman healthOrganellesFlagellaRepeats
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
FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia
Lin J, Le TV, Augspurger K, Tritschler D, Bower R, Fu G, Perrone C, O’Toole E, Mills KV, Dymek E, Smith E, Nicastro D, Porter ME. FAP57/WDR65 targets assembly of a subset of inner arm dyneins and connects to regulatory hubs in cilia. Molecular Biology Of The Cell 2019, 30: 2659-2680. PMID: 31483737, PMCID: PMC6761771, DOI: 10.1091/mbc.e19-07-0367.Peer-Reviewed Original ResearchConceptsInner dynein armsRegulatory complexCryo-electron tomographyInner arm dyneinsCiliary motilityMultiple dynein motorsPrecise spatial organizationAxonemal repeatDocking factorUnique binding siteWD repeatsDynein assemblyAssembly factorsDomain proteinsRegulatory hubDynein complexDynein isoformsDynein subunitsInsertional mutagenesisNew lociRegulatory proteinsDynein motorsDifferent dyneinsDoublet microtubulesTransport factorsDeconstructing Actin Waves
Wu M. Deconstructing Actin Waves. Structure 2019, 27: 1187-1189. PMID: 31390543, DOI: 10.1016/j.str.2019.07.010.Peer-Reviewed Original ResearchIn 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 variationQuantitative High-Speed Video Profiling Discriminates between DNAH11 and HYDIN Variants of Primary Ciliary Dyskinesia
Chioccioli M, Feriani L, Nguyen Q, Kotar J, Dell SD, Mennella V, Amirav I, Cicuta P. Quantitative High-Speed Video Profiling Discriminates between DNAH11 and HYDIN Variants of Primary Ciliary Dyskinesia. American Journal Of Respiratory And Critical Care Medicine 2019, 199: 1436-1438. PMID: 31116566, DOI: 10.1164/rccm.201812-2256le.Peer-Reviewed Original ResearchCiliary Motility DisordersElectron Microscope TomographyGenetic VariationGenotypeHumansVideo Recording
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