Featured Publications
A Screen of Coxiella burnetii Mutants Reveals Important Roles for Dot/Icm Effectors and Host Autophagy in Vacuole Biogenesis
Newton HJ, Kohler LJ, McDonough JA, Temoche-Diaz M, Crabill E, Hartland EL, Roy CR. A Screen of Coxiella burnetii Mutants Reveals Important Roles for Dot/Icm Effectors and Host Autophagy in Vacuole Biogenesis. PLOS Pathogens 2014, 10: e1004286. PMID: 25080348, PMCID: PMC4117601, DOI: 10.1371/journal.ppat.1004286.Peer-Reviewed Original ResearchConceptsHost autophagyTransposon insertionDot/Icm effectorsDot/Icm systemAutophagosome protein LC3Intracellular growth defectPathogen-occupied vacuolesTransposon insertion mutantsVacuole biogenesisEffector proteinsInsertion mutantsModification enzymesGrowth defectArrayed libraryCentral metabolismIcm systemMutantsMolecular mechanismsVisual screenProtein LC3Host cellsIntracellular replicationGenesIntracellular pathogensRegulatory systemPathogen 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 KinasesUbiquitinationCaspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila
Case CL, Kohler LJ, Lima JB, Strowig T, de Zoete MR, Flavell RA, Zamboni DS, Roy CR. Caspase-11 stimulates rapid flagellin-independent pyroptosis in response to Legionella pneumophila. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 1851-1856. PMID: 23307811, PMCID: PMC3562791, DOI: 10.1073/pnas.1211521110.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Vesicular TransportAnimalsApoptosisApoptosis Regulatory ProteinsBone Marrow CellsCalcium-Binding ProteinsCARD Signaling Adaptor ProteinsCarrier ProteinsCaspase 1CaspasesCaspases, InitiatorCells, CulturedCytokinesCytoskeletal ProteinsEnzyme ActivationFlagellinHost-Pathogen InteractionsImmunoblottingLegionella pneumophilaMacrophagesMiceMice, Inbred C57BLMice, KnockoutMutationMyeloid Differentiation Factor 88NecrosisNLR Family, Pyrin Domain-Containing 3 ProteinReceptor, Interferon alpha-betaConceptsCaspase-11 activationCaspase-11Intracellular pathogen Legionella pneumophilaType IV secretion systemDot/IcmAdapter protein TRIFFunctional type IV secretion systemPathogen Legionella pneumophilaCaspase-1 activation pathwayNAIP/NLRC4Activation pathwayLegionella pneumophilaCaspase-11-dependent pyroptosisSecretion systemSevere defectsBacterial flagellinTreatment of macrophagesType I IFN receptorHost componentsIntracellular pathogensMicrobial signaturesPathwayIFN receptorCaspase-1Alternative pathway
2006
NALP3: a key player in caspase-1 activation
Sutterwala F, Ogura Y, Zamboni D, Roy C, Flavell R. NALP3: a key player in caspase-1 activation. Innate Immunity 2006, 12: 251-256. PMID: 16953978, DOI: 10.1177/09680519060120040701.Peer-Reviewed Original ResearchConceptsNLR familyCell death pathwaysNLR family membersAdaptor molecule ASCPro-inflammatory caspasesMultiprotein complexesDeath pathwaysPathogen recognitionCaspase-1 activationKey playersRecent findingsCaspase-1Family membersAuto-inflammatory syndromeActivationAuto-inflammatory disordersFamilyCaspasesGenesMuckle-Wells syndromeBiologyImmune responseProteinMembersFamilial cold auto-inflammatory syndrome
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 hairsERMutants
1999
Modulation of phagosome biogenesis by Legionella pneumophila creates an organelle permissive for intracellular growth
Coers J, Monahan C, Roy C. Modulation of phagosome biogenesis by Legionella pneumophila creates an organelle permissive for intracellular growth. Nature Cell Biology 1999, 1: 451-453. PMID: 10559990, DOI: 10.1038/15687.Peer-Reviewed Original Research
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
1996
Use of Salt to Isolate Legionella pneumophila Mutants Unable to Replicate in Macrophages
VOGEL J, ROY C, ISBERG R. Use of Salt to Isolate Legionella pneumophila Mutants Unable to Replicate in Macrophages. Annals Of The New York Academy Of Sciences 1996, 797: 271-272. PMID: 8993377, DOI: 10.1111/j.1749-6632.1996.tb52975.x.Peer-Reviewed Original Research
1993
Legionella pneumophila: factors involved in the route and response to an intracellular niche.
Isberg R, Rankin S, Roy C, Swanson M, Berger K. Legionella pneumophila: factors involved in the route and response to an intracellular niche. Infectious Agents And Disease 1993, 2: 220-3. PMID: 8173798.Peer-Reviewed Original Research