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 mutation
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. interrogansFlagellaBacteria
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 pathogensAnalysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi
Zhang K, Qin Z, Chang Y, Liu J, Malkowski MG, Shipa S, Li L, Qiu W, Zhang J, Li C. Analysis of a flagellar filament cap mutant reveals that HtrA serine protease degrades unfolded flagellin protein in the periplasm of Borrelia burgdorferi. Molecular Microbiology 2019, 111: 1652-1670. PMID: 30883947, PMCID: PMC6561814, DOI: 10.1111/mmi.14243.Peer-Reviewed Original ResearchConceptsPeriplasmic flagellaFliD mutantFlagellin proteinMajor flagellin proteinLyme disease spirochete Borrelia burgdorferiFlagellar cap proteinFlagellar cap protein FliDFlagellar filament assemblyFlagella-deficient mutantsMutant cellsCAP mutantsFlaB proteinsPeriplasmFilament assemblyCap proteinB. burgdorferiFlagellar filamentsGenetic studiesMutantsBorrelia burgdorferiHtrASerine proteasesFliDFlagellin polymerizationSpirochete Borrelia burgdorferi
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
2016
A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete
Wunder EA, Figueira CP, Benaroudj N, Hu B, Tong BA, Trajtenberg F, Liu J, Reis MG, Charon NW, Buschiazzo A, Picardeau M, Ko AI. A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete. Molecular Microbiology 2016, 101: 457-470. PMID: 27113476, PMCID: PMC4979076, DOI: 10.1111/mmi.13403.Peer-Reviewed Original ResearchConceptsTraverse tissue barriersHamster modelTarget organsSystemic infectionClinical isolatesLeptospira spirochetesTranslational motilityL. interrogansCell morphologyTissue barriersMotilityLeptospiraPeriplasmic flagellaSpirochetesVirulence phenotypesProtein AHelical cell morphologyInfectionDiseaseLeptospirosisPathogen L. interrogans