Featured Publications
Multiple Legionella pneumophila effector virulence phenotypes revealed through high-throughput analysis of targeted mutant libraries
Shames SR, Liu L, Havey JC, Schofield WB, Goodman AL, Roy CR. Multiple Legionella pneumophila effector virulence phenotypes revealed through high-throughput analysis of targeted mutant libraries. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e10446-e10454. PMID: 29133401, PMCID: PMC5715750, DOI: 10.1073/pnas.1708553114.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCytotoxicity, ImmunologicDisease Models, AnimalFemaleGene Expression Regulation, BacterialHigh-Throughput Nucleotide SequencingHost-Pathogen InteractionsHumansLegionella pneumophilaLegionnaires' DiseaseLoss of Function MutationMiceMice, Inbred C57BLMutagenesis, InsertionalPhenotypeVirulenceConceptsCultured host cellsHost cellsEffector proteinsHost immune systemFunction mutationsVirulence phenotypesSevere pneumoniaInfected miceBacterial clearanceEffector mutantsLarge cohortMouse modelDot/Icm type IV secretion systemImmune systemType IV secretion systemScreen resultsEffector protein activityDifferent effector proteinsGenetic complementation studiesLegionnaires' diseaseCausative agentHost pathogenesisDifferent virulence phenotypesInfectionDiseaseThe 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 ResearchPathogen signatures activate a ubiquitination pathway that modulates the function of the metabolic checkpoint kinase mTOR
Ivanov SS, Roy CR. Pathogen signatures activate a ubiquitination pathway that modulates the function of the metabolic checkpoint kinase mTOR. Nature Immunology 2013, 14: 1219-1228. PMID: 24121838, PMCID: PMC3839319, DOI: 10.1038/ni.2740.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell LineCells, CulturedCytokinesEukaryotic Initiation Factor-4EGene ExpressionHost-Pathogen InteractionsImmunoblottingLegionella pneumophilaLegionnaires' DiseaseMacrophagesMiceMolecular Sequence DataMutationProto-Oncogene Proteins c-aktReverse Transcriptase Polymerase Chain ReactionRNA InterferenceSignal TransductionTOR Serine-Threonine KinasesUbiquitinationModulation of Rab GTPase function by a protein phosphocholine transferase
Mukherjee S, Liu X, Arasaki K, McDonough J, Galán JE, Roy CR. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 2011, 477: 103-106. PMID: 21822290, PMCID: PMC3206611, DOI: 10.1038/nature10335.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsChlorocebus aethiopsCOS CellsDiacylglycerol CholinephosphotransferaseGuanine Nucleotide Exchange FactorsHEK293 CellsHost-Pathogen InteractionsHumansLegionella pneumophilaLegionnaires' DiseaseMass SpectrometryProtein Processing, Post-TranslationalRab GTP-Binding ProteinsThe Legionella Effector RavZ Inhibits Host Autophagy Through Irreversible Atg8 Deconjugation
Choy A, Dancourt J, Mugo B, O’Connor T, Isberg RR, Melia TJ, Roy CR. The Legionella Effector RavZ Inhibits Host Autophagy Through Irreversible Atg8 Deconjugation. Science 2012, 338: 1072-1076. PMID: 23112293, PMCID: PMC3682818, DOI: 10.1126/science.1227026.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAutophagyAutophagy-Related Protein 7Autophagy-Related Protein 8 FamilyAutophagy-Related ProteinsBacterial ProteinsCell Culture TechniquesCysteine ProteasesGene DeletionGlycineHEK293 CellsHost-Pathogen InteractionsHumansHydrolysisLegionella pneumophilaLegionnaires' DiseaseMicrofilament ProteinsPhagosomesUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesConceptsATG8 proteinsIntracellular pathogen Legionella pneumophilaPathogen Legionella pneumophilaAdjacent aromatic residuesCarboxyl-terminal glycine residueAutophagosome membraneEukaryotic cellsAutophagy pathwayGlycine residueAromatic residuesIntracellular pathogensRavZAutophagyProteinLegionella pneumophilaSpecific mechanismsResiduesPathogensATG3MicrobesAtg7CytosolVacuolesPathwayPneumophila
2000
Identification of Icm protein complexes that play distinct roles in the biogenesis of an organelle permissive for Legionella pneumophila intracellular growth
Coers J, Kagan J, Matthews M, Nagai H, Zuckman D, Roy C. Identification of Icm protein complexes that play distinct roles in the biogenesis of an organelle permissive for Legionella pneumophila intracellular growth. Molecular Microbiology 2000, 38: 719-736. PMID: 11115108, DOI: 10.1046/j.1365-2958.2000.02176.x.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCarrier ProteinsHumansLegionella pneumophilaLegionnaires' DiseaseLysosomesMacrophages, AlveolarOrganellesConceptsPhagosome traffickingTransport apparatusHost cellsProtein-protein interactionsSubset of genesGel overlay analysisDistinct phenotypic categoriesPhagocytic host cellsIcm genesTranslocation channelReplicative organelleTwo-hybridProtein complexesSpecialized organellesTransporter functionIntracellular growthMolecular levelDistinct rolesVirulence determinantsGenesPore formationBacterial pathogensBiogenesisPhenotypic categoriesLegionella pneumophila