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 activationMembraneLegionella pneumophila proteins that regulate Rab1 membrane cycling
Ingmundson A, Delprato A, Lambright DG, Roy CR. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 2007, 450: 365-369. PMID: 17952054, DOI: 10.1038/nature06336.Peer-Reviewed Original ResearchConceptsDrrA proteinRab1 functionMembrane cyclingGTPase-activating protein activityIntracellular pathogen Legionella pneumophilaRecruitment of Rab1Pathogen-occupied vacuolesPathogen Legionella pneumophilaDistinct biochemical reactionsL. pneumophilaLegionella pneumophilaRab1 activityRab1 activationRab proteinsEukaryotic cellsExchange factorGTP hydrolysisProtein activityRab1Membrane functionBacterial replicationProteinBiochemical reactionsPneumophilaVacuolesAnkyrin Repeat Proteins Comprise a Diverse Family of Bacterial Type IV Effectors
Pan X, Lührmann A, Satoh A, Laskowski-Arce MA, Roy CR. Ankyrin Repeat Proteins Comprise a Diverse Family of Bacterial Type IV Effectors. Science 2008, 320: 1651-1654. PMID: 18566289, PMCID: PMC2514061, DOI: 10.1126/science.1158160.Peer-Reviewed Original ResearchConceptsSecretion systemL. pneumophila-containing vacuoleIntracellular pathogen Legionella pneumophilaHost cellsDifferent bacterial proteinsType IV secretion systemMicrotubule-dependent vesicular transportEukaryotic host cellsType IV effectorsPathogen Legionella pneumophilaSpecialized secretion systemsAnkyrin Repeat ProteinsANK proteinsEukaryotic cellsHomology domainEffector proteinsEukaryotic factorsRepeat proteinsInfection of macrophagesVesicular transportBacterial proteinsLate endosomesDiverse familyProteinLegionella pneumophilaThe Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion
Arasaki K, Toomre DK, Roy CR. The Legionella pneumophila Effector DrrA Is Sufficient to Stimulate SNARE-Dependent Membrane Fusion. Cell Host & Microbe 2012, 11: 46-57. PMID: 22264512, PMCID: PMC3266541, DOI: 10.1016/j.chom.2011.11.009.Peer-Reviewed Original ResearchConceptsMembrane transport pathwaysEndoplasmic reticulumSyntaxin proteinsFusion of ERMembrane fusionSNARE-dependent membrane fusionBacterial pathogen Legionella pneumophilaPathogen-containing vacuolesSNARE protein Sec22bIntracellular bacterial pathogen Legionella pneumophilaPathogen Legionella pneumophilaFusion of vesiclesRab1 activationNoncanonical pairingTransport pathwaysRab1 GTPasePlasma membraneVesicle fusionOrganellesDrrASec22bVesiclesLegionella pneumophilaProteinVacuolesThe 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
2010
Inhibition of pathogen-induced apoptosis by a Coxiella burnetii type IV effector protein
Lührmann A, Nogueira CV, Carey KL, Roy CR. Inhibition of pathogen-induced apoptosis by a Coxiella burnetii type IV effector protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 18997-19001. PMID: 20944063, PMCID: PMC2973885, DOI: 10.1073/pnas.1004380107.Peer-Reviewed Original ResearchConceptsPathogen-induced apoptosisEffector proteinsMammalian hostsL. pneumophila effector proteinsType IV effector proteinsHost cellsType IV secretion systemMammalian host cellsL. pneumophilaGain of functionProtein repertoireOrganelle traffickingRepeat familyDistinct hostsSecretion systemInfection strategiesProtozoan hostsApoptosis pathwayIntracellular bacteriaIntracellular replicationVirulence determinantsProteinLegionella pneumophilaApoptosisPathogens
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
The 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