Featured Publications
The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs
Horenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. Developmental Cell 2015, 34: 569-576. PMID: 26343456, PMCID: PMC4594837, DOI: 10.1016/j.devcel.2015.08.010.Peer-Reviewed Original ResearchConceptsATG8 proteinsIntracellular pathogen Legionella pneumophilaPre-autophagosomal structureAtg8/LC3 proteinsPathogen Legionella pneumophilaHigh-curvature membranesMembrane transport pathwaysCytosol of cellsEffector proteinsCatalytic domainHost cytosolRavZAutophagy proteinsLC3 proteinPathogenic microbesSubstrate affinityProteinIntermediate membraneLegionella pneumophilaAutophagosomesAutophagyCytosolTransport pathwaysInterfacial activationMembrane
2024
The T4bSS of Legionella features a two-step secretion pathway with an inner membrane intermediate for secretion of transmembrane effectors.
Malmsheimer S, Grin I, Bohn E, Franz-Wachtel M, Macek B, Sahr T, Smollich F, Chetrit D, Meir A, Roy C, Buchrieser C, Wagner S. The T4bSS of Legionella features a two-step secretion pathway with an inner membrane intermediate for secretion of transmembrane effectors. PLOS Pathogens 2024, 20: e1012118. PMID: 39546547, PMCID: PMC11602083, DOI: 10.1371/journal.ppat.1012118.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCell MembraneLegionella pneumophilaMembrane ProteinsProtein TransportSecretory PathwayType IV Secretion SystemsConceptsEukaryotic host cellsEffector proteinsMembrane intermediatesC-terminal secretion signalHost cellsSoluble effector proteinsCytoplasmic sideBacterial inner membraneMechanism of secretionSecretion systemSecretion signalPeriplasmic loopTransmembrane effectorSecretion pathwayT4BSSInner membraneSubcellular locationIntracellular survivalMembrane targetingProtein complexesEfficient translocationBacterial cellsProteomic analysisL. pneumophilaSecretion process
2001
How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane.
Tilney L, Harb O, Connelly P, Robinson C, Roy C. How the parasitic bacterium Legionella pneumophila modifies its phagosome and transforms it into rough ER: implications for conversion of plasma membrane to the ER membrane. Journal Of Cell Science 2001, 114: 4637-50. PMID: 11792828, DOI: 10.1242/jcs.114.24.4637.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCarrier ProteinsCell FractionationCell MembraneGram-Positive BacteriaHumansIntracellular MembranesLegionella pneumophilaLipid MetabolismLysosomesMembrane ProteinsMicroscopy, ElectronMitochondriaMolecular ChaperonesMutationOrganellesPhagosomesRibosomesTime FactorsU937 CellsConceptsPhagosomal membraneRough endoplasmic reticulumRough ERL. pneumophilaL. pneumophila mutantsBacterium Legionella pneumophilaMinutes of infectionLegionella pneumophilaInfected macrophagesER membraneCellular processesMitochondrial membranePlasma membraneER vesiclesEndoplasmic reticulumMacrophage infectionPhagosomesLack of cholesterolMitochondriaPneumophilaMembraneTiny hairsERMutantsThe DotA protein from Legionella pneumophila is secreted by a novel process that requires the Dot/Icm transporter
Nagai H, Roy C. The DotA protein from Legionella pneumophila is secreted by a novel process that requires the Dot/Icm transporter. The EMBO Journal 2001, 20: 5962-5970. PMID: 11689436, PMCID: PMC125688, DOI: 10.1093/emboj/20.21.5962.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBiological TransportCarrier ProteinsCell MembraneCulture Media, ConditionedElectrophoresis, Polyacrylamide GelHost-Parasite InteractionsImmunoblottingLegionella pneumophilaMacromolecular SubstancesMembrane ProteinsMolecular Sequence DataOrganellesSequence Analysis, ProteinConceptsDot/icm genesDotA proteinIcm genesDot/Icm transporterPolytopic membrane proteinsDot/IcmEukaryotic host cellsN-terminal sequencingAmino acid leader peptideLegionella pneumophilaSecretion apparatusMembrane proteinsLeader peptideMembrane vesiclesProtein secretionHost cellsProteinBacterial replicationGenesTransportersPneumophilaUnique processOrganellesCulture supernatantsSecretion
1999
Pore‐forming activity is not sufficient for Legionella pneumophila phagosome trafficking and intracellular growth
Zuckman D, Hung J, Roy C. Pore‐forming activity is not sufficient for Legionella pneumophila phagosome trafficking and intracellular growth. Molecular Microbiology 1999, 32: 990-1001. PMID: 10361301, DOI: 10.1046/j.1365-2958.1999.01410.x.Peer-Reviewed Original ResearchConceptsPhagosome traffickingPhagosome-lysosome fusionIntracellular growthLysosome fusionEukaryotic cellular processesInsertion of poresPore-forming activityL. pneumophila mutantsHost cell cytoplasmCellular processesMammalian cellsReplicative nicheSimilar cytolytic activityGene productsPhagosome membraneIntracellular bacteriaTraffickingCell cytoplasmEffector moleculesBacterial pathogensLegionella pneumophilaMacrophage membraneVirulent bacteriaBacteriaFusion inhibition
1998
Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake
Roy C, Berger K, Isberg R. Legionella pneumophila DotA protein is required for early phagosome trafficking decisions that occur within minutes of bacterial uptake. Molecular Microbiology 1998, 28: 663-674. PMID: 9632267, DOI: 10.1046/j.1365-2958.1998.00841.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBacterial ProteinsCell LineFluorescent Antibody TechniqueGTP-Binding ProteinsHumansLegionella pneumophilaLysosome-Associated Membrane GlycoproteinsLysosomesMacrophagesMembrane FusionMembrane GlycoproteinsMembrane ProteinsMiceMutationPhagosomesPlasmidsRab GTP-Binding ProteinsRab7 GTP-Binding ProteinsConceptsDotA mutantsL. pneumophila phagosomeLAMP-1DotA proteinL. pneumophilaMembrane-bound compartmentsLysosomal glycoprotein LAMP-1Bacterial pathogensIntracellular bacterial pathogenReplicative phagosomeSmall GTPVacuolar membraneEndocytic pathwayProtein Rab7Fusion eventsMutant bacteriaMolecular basisGenetic studiesBacterial uptakeMutantsPhagosomesTrafficking profilesContinuous expressionIntracellular sitesMacrophage uptake
1997
Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages
Roy C, Isberg R. Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages. Infection And Immunity 1997, 65: 571-578. PMID: 9009315, PMCID: PMC176098, DOI: 10.1128/iai.65.2.571-578.1997.Peer-Reviewed Original ResearchConceptsDotA mutantsAmino acidsMembrane proteinsIntegral cytoplasmic membrane proteinLarge periplasmic domainInner membrane proteinCarboxyl-terminal cytoplasmic domainIntracellular growthCytoplasmic membrane proteinAlkaline phosphatase fusionsL. pneumophila pathogenesisIntracellular growth defectMembrane-spanning domainsStructure-function analysisProtein fractionation studiesPeriplasmic domainDotA proteinTranslational fusionGrowth defectCytoplasmic domainInner membraneHybrid proteinCytoplasmic regionDotA geneC-terminus