2021
The 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
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 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 pathogensStructural 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
2016
Imaging the Motility and Chemotaxis Machineries in Helicobacter pylori by Cryo-Electron Tomography
Qin Z, Lin WT, Zhu S, Franco AT, Liu J. Imaging the Motility and Chemotaxis Machineries in Helicobacter pylori by Cryo-Electron Tomography. Journal Of Bacteriology 2016, 199: 10.1128/jb.00695-16. PMID: 27849173, PMCID: PMC5237115, DOI: 10.1128/jb.00695-16.Peer-Reviewed Original ResearchCryo-electron tomographyChemotaxis arraysUnipolar flagellaBacterial pathogensFlagella-driven motilityMultiple unipolar flagellaNovel structural insightsFlagellar assemblyChemotaxis machineryFlagellar poleAssembly intermediatesFlagellar rotationFlagellar motorCell envelopeStructural insightsMembrane sheathSheathed flagellumMolecular mechanismsUnique motilityH. pylori cellsFlagellaSitu structureHigh-viscosity environmentsPylori cellsMotility