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
Exploitation of a Bacterium-Encoded Lytic Transglycosylase by a Human Oral Lytic Phage To Facilitate Infection
Cen L, Chang Y, Bedree JK, Ma Y, Zhong Q, Utter DR, Dong PT, Lux R, Bor B, Liu J, McLean JS, Le S, He X. Exploitation of a Bacterium-Encoded Lytic Transglycosylase by a Human Oral Lytic Phage To Facilitate Infection. Journal Of Virology 2022, 96: e01063-22. PMID: 36000841, PMCID: PMC9472602, DOI: 10.1128/jvi.01063-22.Peer-Reviewed Original ResearchConceptsLytic transglycosylaseLytic phagesPhage receptorsOral phageRemarkable host specificityHuman oral microbiomeSimilar expression levelsPeptidoglycan remodelingWhole-genome sequencingMutant backgroundBacterial physiologyHost specificityMicrobial communitiesSurface-grown cellsPhage populationsSensitive phenotypeBacterial hostsOral microbiomePeptidoglycan structureWild typeMetagenomic analysisMutantsSpontaneous mutantsXH001Frameshift mutationTranscriptome of Epibiont Saccharibacteria Nanosynbacter lyticus Strain TM7x During the Establishment of Symbiosis
Hendrickson EL, Bor B, Kerns KA, Lamont EI, Chang Y, Liu J, Cen L, Schulte F, Hardt M, Shi W, He X, McLean JS. Transcriptome of Epibiont Saccharibacteria Nanosynbacter lyticus Strain TM7x During the Establishment of Symbiosis. Journal Of Bacteriology 2022, 204: e00112-22. PMID: 35975994, PMCID: PMC9487520, DOI: 10.1128/jb.00112-22.Peer-Reviewed Original ResearchConceptsCandidate Phyla RadiationEstablishment of symbiosisStable symbiosisStress-related genesGene expressionReduced genomePeptidoglycan biosynthesisHost bacteriaHuman microbiomeBiosynthesis gene expressionMonophyletic radiationCell sizeEffector genesPartitioning genesObligate parasitesUnique organismsBiosynthetic pathwayHigher gene expressionCell shapeTransporter geneCell wallObligate epibiontsLow expressionSymbiosisCell cycleIn situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts
Cai S, Wu Y, Guillén-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. In situ architecture of the lipid transport protein VPS13C at ER–lysosome 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/lysosomes
2021
Role 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. interrogansFlagellaBacteriaThe 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 ResearchConceptsPeptidoglycan-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
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 Research
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 pathogens
2018
Visualization 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 ResearchConceptsCryo-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 associationTranslocationBacteria
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 Research
2008
Integrin αIIbβ3 in a Membrane Environment Remains the Same Height after Mn2+ Activation when Observed by Cryoelectron Tomography
Ye F, Liu J, Winkler H, Taylor KA. Integrin αIIbβ3 in a Membrane Environment Remains the Same Height after Mn2+ Activation when Observed by Cryoelectron Tomography. Journal Of Molecular Biology 2008, 378: 976-986. PMID: 18405917, PMCID: PMC2614134, DOI: 10.1016/j.jmb.2008.03.014.Peer-Reviewed Original Research