Featured Publications
The Machinery at Endoplasmic Reticulum-Plasma Membrane Contact Sites Contributes to Spatial Regulation of Multiple Legionella Effector Proteins
Hubber A, Arasaki K, Nakatsu F, Hardiman C, Lambright D, De Camilli P, Nagai H, Roy CR. The Machinery at Endoplasmic Reticulum-Plasma Membrane Contact Sites Contributes to Spatial Regulation of Multiple Legionella Effector Proteins. PLOS Pathogens 2014, 10: e1004222. PMID: 24992562, PMCID: PMC4081824, DOI: 10.1371/journal.ppat.1004222.Peer-Reviewed Original Research
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 ResearchConceptsEukaryotic 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