2000
Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice
Grigera P, Marzocca M, Capozzo A, Buonocore L, Donis R, Rose J. Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice. Virus Research 2000, 69: 3-15. PMID: 10989181, DOI: 10.1016/s0168-1702(00)00164-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodies, ViralBase SequenceCattleCell LineChimeraCricetinaeDiarrhea Viruses, Bovine ViralDNA, RecombinantFemaleMembrane GlycoproteinsMiceMice, Inbred BALB CNeutralization TestsRecombinant ProteinsVaccines, SyntheticVesicular stomatitis Indiana virusViral Envelope ProteinsViral VaccinesConceptsBovine viral diarrhea virus (BVDV) E2BALB/c miceRecombinant vesicular stomatitis virusViral-induced diseasesC miceE2 antibodiesBVDV antibodiesVesicular stomatitis virusHigh avidityBVDV E2Recombinant E2Infected cellsDays post inoculationG glycoproteinE2Stomatitis virusMiceAntibodiesImmunofluorescence microscopyPost inoculationRecombinant particlesBHK21 cellsCellsSymptomsInfection
1999
Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion
Kahn J, Schnell M, Buonocore L, Rose J. Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion. Virology 1999, 254: 81-91. PMID: 9927576, DOI: 10.1006/viro.1998.9535.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCricetinaeCytoplasmGene ExpressionGenetic VectorsGlycoproteinsHN ProteinHumansMembrane FusionMolecular Sequence DataRecombinant Fusion ProteinsRespiratory Syncytial Virus, HumanTumor Cells, CulturedVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsViral ProteinsVirionConceptsRecombinant vesicular stomatitis virusVesicular stomatitis virusRSV fusion proteinRSV F glycoproteinRSV vaccineF recombinantsRSV glycoproteinsRSV proteinsEnvelope glycoproteinVirus attachmentFusion (F) envelope glycoproteinsF glycoproteinG glycoproteinStomatitis virusLarge syncytiaGlycoproteinPH-independent pathwayCell surfaceCell fusionCytoplasmic tail sequencesVSV G.Endosomal pHFusion activityVaccineFusion protein
1998
A Plasma Membrane Localization Signal in the HIV-1 Envelope Cytoplasmic Domain Prevents Localization at Sites of Vesicular Stomatitis Virus Budding and Incorporation into VSV Virions
Johnson J, Rodgers W, Rose J. A Plasma Membrane Localization Signal in the HIV-1 Envelope Cytoplasmic Domain Prevents Localization at Sites of Vesicular Stomatitis Virus Budding and Incorporation into VSV Virions. Virology 1998, 251: 244-252. PMID: 9837788, DOI: 10.1006/viro.1998.9429.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell MembraneCells, CulturedCricetinaeCytoplasmGene Products, envHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicroscopy, ConfocalMolecular Sequence DataProtein Sorting SignalsRecombinant ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsVSV virionsMembrane-proximal amino acidsMembrane localization signalAmino acidsVesicular stomatitis virus (VSV) virionsLocalization signalMembrane domainsG-tailsCytoplasmic tailVirus buddingPrevents localizationVirus virionsMutantsVSV proteinsProteinConfocal microscopyVSV recombinantsEnvelope proteinVSV glycoproteinHuman Immunodeficiency Virus Type 1 EnvVirionsHIV-1 envelope proteinEnv proteinTailHybridsGeneration of mucosal cytotoxic T cells against soluble protein by tissue-specific environmental and costimulatory signals
Kim S, Reed D, Olson S, Schnell M, Rose J, Morton P, Lefrançois L. Generation of mucosal cytotoxic T cells against soluble protein by tissue-specific environmental and costimulatory signals. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 10814-10819. PMID: 9724787, PMCID: PMC27978, DOI: 10.1073/pnas.95.18.10814.Peer-Reviewed Original ResearchConceptsCD8 T cellsT cellsT lymphocytesPrimary CD8 T cell responseCD8 T cell responsesMucosal cytotoxic T lymphocytesPeripheral CD8 T cellsMajor histocompatibility complex class IActivation of peripheralMucosal T cellsT cell responsesHistocompatibility complex class ICytotoxic T cellsCytotoxic T lymphocytesT cell generationComplex class IInflammatory mediatorsPeripheral toleranceAntigen administrationCostimulatory requirementsMucosal sitesAdjuvant effectB7-1B7-2Inflammatory signalsRequirement for a non‐specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus
Schnell M, Buonocore L, Boritz E, Ghosh H, Chernish R, Rose J. Requirement for a non‐specific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus. The EMBO Journal 1998, 17: 1289-1296. PMID: 9482726, PMCID: PMC1170477, DOI: 10.1093/emboj/17.5.1289.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCD4 AntigensCell LineCell MembraneCricetinaeCytopathogenic Effect, ViralCytoplasmHumansMembrane GlycoproteinsMolecular Sequence DataMutationRecombinant Fusion ProteinsSequence DeletionSerial PassageVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsVirionConceptsCytoplasmic domainEfficient buddingAmino acidsCytoplasmic domain deletion mutantEfficient virus buddingShort cytoplasmic domainCytoplasmic domain sequencesDomain deletion mutantVesicular stomatitis virus glycoproteinChimeric G proteinsTransmembrane domainDeletion mutantsInternal viral componentsVirus buddingGlycoprotein arrayVesicular stomatitis virusDomain sequencesViral buddingVirion morphologyG proteinsMatrix proteinsVSV GHuman CD4 proteinForeign sequencesBudding
1996
Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗)
Turi T, Mueller U, Sazer S, Rose J. Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗). Journal Of Biological Chemistry 1996, 271: 9166-9171. PMID: 8621569, DOI: 10.1074/jbc.271.15.9166.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBase SequenceBrefeldin ACell CompartmentationConsensus SequenceCyclopentanesDNA PrimersDrug Resistance, MicrobialFungal ProteinsGenes, FungalGolgi ApparatusGTP-Binding ProteinsMolecular Sequence DataNuclear ProteinsPhosphoproteinsRan GTP-Binding ProteinRestriction MappingSchizosaccharomycesSequence AlignmentSequence Homology, Amino AcidConceptsNuclear pore complexWild type SchizosaccharomycesPore complexS. pombeSchizosaccharomyces pombeProtein RanBP1Essential proteinsGolgi complexEndoplasmic reticulumProtein secretionPeptide motifsMultiple copiesNovel mechanismGenesProteinPombeA ResistanceBrefeldinDrug resistanceSchizosaccharomycesYrb1RanBP1HomologyComplexesReticulumNormal Replication of Vesicular Stomatitis Virus without C Proteins
KRETZSCHMAR E, PELUSO R, SCHNELL M, WHITT M, ROSE J. Normal Replication of Vesicular Stomatitis Virus without C Proteins. Virology 1996, 216: 309-316. PMID: 8607260, DOI: 10.1006/viro.1996.0066.Peer-Reviewed Original ResearchConceptsP geneWild-type virusNormal replicationSmall basic proteinP protein sequenceSingle base changeNew Jersey serotypeWild-type virus particlesInsect vectorsVesicular stomatitis virusC proteinStop codonViral mRNAsVSV growthInfectious cloneBase changesMutant virusProteinGenesStomatitis virusViral pathogenesisBasic proteinM proteinVirus particlesTissue culture
1995
Characterization of a Novel Schizosaccharomyces pombe Multidrug Resistance Transporter Conferring Brefeldin A Resistance
Turi T, Rose J. Characterization of a Novel Schizosaccharomyces pombe Multidrug Resistance Transporter Conferring Brefeldin A Resistance. Biochemical And Biophysical Research Communications 1995, 213: 410-418. PMID: 7646493, DOI: 10.1006/bbrc.1995.2147.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceATP-Binding Cassette TransportersBase SequenceBinding SitesBrefeldin ACloning, MolecularCyclopentanesDNA, FungalDrug Resistance, MultipleFungal ProteinsMolecular Sequence DataOpen Reading FramesPancreatitis-Associated ProteinsRestriction MappingSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence AnalysisSequence HomologyConceptsTranscription factorsHbA2 expressionWild-type S. pombeS. pombe proteinPap1 transcription factorSignificant sequence similarityWild type SchizosaccharomycesMultiple transcription factorsPombe proteinsCRM1 genesS. pombeSequence similarityMammalian cellsTransport proteinsDifferent genesMutant strainBrefeldin AGolgi complexEndoplasmic reticulumProtein secretionGenesMultiple copiesSchizosaccharomycesCRM1A Resistance
1994
Stimulation of Heterologous Protein Degradation by the Vpu Protein of HIV-1 Requires the Transmembrane and Cytoplasmic Domains of CD4
Buonocore L, Turi T, Crise B, Rose J. Stimulation of Heterologous Protein Degradation by the Vpu Protein of HIV-1 Requires the Transmembrane and Cytoplasmic Domains of CD4. Virology 1994, 204: 482-486. PMID: 8091684, DOI: 10.1006/viro.1994.1560.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensGlycoproteinsHeLa CellsHIV-1Human Immunodeficiency Virus ProteinsHumansMembrane GlycoproteinsMolecular Sequence DataProtein Structure, TertiaryRecombinant Fusion ProteinsRecombinant ProteinsViral Envelope ProteinsViral Regulatory and Accessory ProteinsConceptsCytoplasmic domainTransmembrane domainHybrid proteinHeterologous protein degradationVesicular stomatitis virus glycoproteinRapid degradationAdditional hybridsProtein degradationExtracellular domainProtein VpuRelated sequencesVpu proteinDegradation systemEndoplasmic reticulumVSV GVpu expressionProteinVpuTransmembraneVirus glycoproteinRecent studiesDomainHuman immunodeficiency virus type 1Immunodeficiency virus type 1DegradationBrefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance.
Turi T, Webster P, Rose J. Brefeldin A sensitivity and resistance in Schizosaccharomyces pombe. Isolation of multiple genes conferring resistance. Journal Of Biological Chemistry 1994, 269: 24229-24236. PMID: 7929079, DOI: 10.1016/s0021-9258(19)51072-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBrefeldin ACyclopentanesDrug Resistance, MicrobialFungal ProteinsGolgi ApparatusKaryopherinsMolecular Sequence DataMutationPancreatitis-Associated ProteinsPhenotypePlasmidsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSchizosaccharomycesSequence Homology, Amino AcidConceptsBFA resistanceEffects of BFABrefeldin AGolgi complexMammalian cellsTranscription factor Pap1Fission yeast SchizosaccharomycesFungal metabolite brefeldin ASeparate linkage groupsWild-type cellsChromatin structureYeast SchizosaccharomycesSchizosaccharomyces pombeAP1 proteinLinkage groupsGolgi morphologyAnimal cellsMultiple genesDifferent genesGenetic analysisEndoplasmic reticulumProtein secretionGenesType cellsMutantsSignals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction.
Rodgers W, Crise B, Rose J. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. PMID: 8035816, PMCID: PMC359057, DOI: 10.1128/mcb.14.8.5384.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell CompartmentationDNA PrimersGlycolipidsGlycosylphosphatidylinositolsHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataMutagenesis, Site-DirectedMyristatesPalmitatesProteinsProtein-Tyrosine KinasesStructure-Activity RelationshipConceptsProtein tyrosine kinasesCertain protein tyrosine kinasesTyrosine kinaseMembrane fractionSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorGlycosyl phosphatidylinositolKinaseP56lckCell typesHeLa cellsMDCK cellsGPIProteinGentle disruptionInteractions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids
Chong L, Rose J. Interactions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids. Journal Of Virology 1994, 68: 441-447. PMID: 8254754, PMCID: PMC236304, DOI: 10.1128/jvi.68.1.441-447.1994.Peer-Reviewed Original ResearchConceptsMembrane associationPlasma membraneAmino-terminal basic domainVesicular stomatitis virusWild-type M proteinCellular membranesMatrix proteinsVesicular stomatitis virus matrix proteinM proteinStable membrane associationTruncated M proteinsVirus matrix proteinVSV nucleocapsidsBasic domainAmino terminusNucleocapsid bindingNucleocapsid interactionMembrane fractionVSV proteinsAmino acidsMembrane specificityProteinStomatitis virusNucleocapsidsMembrane
1992
Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.
Crise B, Rose J. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. Journal Of Biological Chemistry 1992, 267: 13593-13597. PMID: 1618861, DOI: 10.1016/s0021-9258(18)42253-3.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomainFc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization.
Miettinen H, Matter K, Hunziker W, Rose J, Mellman I. Fc receptor endocytosis is controlled by a cytoplasmic domain determinant that actively prevents coated pit localization. Journal Of Cell Biology 1992, 116: 875-888. PMID: 1734021, PMCID: PMC2289334, DOI: 10.1083/jcb.116.4.875.Peer-Reviewed Original Research
1990
Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum
Buonocore L, Rose J. Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum. Nature 1990, 345: 625-628. PMID: 2190096, DOI: 10.1038/345625a0.Peer-Reviewed Original ResearchConceptsCD4 moleculeHIV glycoproteinSoluble CD4 moleculesHuman immunodeficiency virusCellular CD4 receptorWild-type CD4Human T cellsInfectious HIVCD4 cellsImmunodeficiency virusSoluble CD4T cellsTherapeutic strategiesCD4 receptorImmunization procedureEnvelope glycoproteinVirus entrySurface expressionCD4HIVIdeal targetEndoplasmic reticulumVirusExpressionCellsShort related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase.
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. PMID: 2109184, PMCID: PMC360530, DOI: 10.1128/mcb.10.5.1853.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, Differentiation, T-LymphocyteBase SequenceCD4 AntigensCD8 AntigensCysteineCytoplasmDNA Mutational AnalysisHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataProtein BindingProtein-Tyrosine KinasesSignal TransductionStructure-Activity RelationshipConceptsAmino-terminal domainTyrosine protein kinaseCytoplasmic domainProtein kinaseBinding of p56lckCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationCD8 alphaAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsAlpha proteinRelated sequencesAcid residuesCD4 sequencesP56lckGlycoprotein CD4HeLa cellsProteinKinase
1989
Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum.
Zagouras P, Rose J. Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum. Journal Of Cell Biology 1989, 109: 2633-2640. PMID: 2592401, PMCID: PMC2115906, DOI: 10.1083/jcb.109.6.2633.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumSEKDEL sequenceSecretory proteinsSequence Ser-GluAmino acidsMonkey COS cellsOligonucleotide-directed mutagenesisLast amino acidFirst amino acidProtein exitIndirect immunofluorescence microscopyAnimal cellsCOS cellsCOOH terminusAlpha subunitProtein structureGolgi apparatusLys-AspImmunofluorescence microscopyOligosaccharide processingProteinReticulumSEKDELSer-GluSpecific interactionsOligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
Crise B, Ruusala A, Zagouras P, Shaw A, Rose J. Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1989, 63: 5328-5333. PMID: 2555557, PMCID: PMC251199, DOI: 10.1128/jvi.63.12.5328-5333.1989.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosaminidaseAmino Acid SequenceBase SequenceCentrifugation, Density GradientCodonElectrophoresis, Polyacrylamide GelGlycolipidsHeLa CellsHumansKineticsMacromolecular SubstancesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMolecular Sequence DataRestriction MappingSolubilityVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsG proteinsWild-type G proteinAmino acidsC-terminal amino acidsVesicular stomatitis virus glycoproteinMutant proteinsCytoplasmic domainAnchor sequenceExtracellular domainGolgi apparatusEndoplasmic reticulumCell surfaceTrimer formationProteinPhospholipase C.TransmembraneVirus glycoproteinSoluble formStructural informationSequenceGlycoproteinNormal transmembraneRate of transportGlycoprotein formThy-1.1The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResiduesGlycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant
Whitt M, Chong L, Rose J. Glycoprotein cytoplasmic domain sequences required for rescue of a vesicular stomatitis virus glycoprotein mutant. Journal Of Virology 1989, 63: 3569-3578. PMID: 2547986, PMCID: PMC250946, DOI: 10.1128/jvi.63.9.3569-3578.1989.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsAmino acidsWild-type G proteinNormal cytoplasmic domainG protein mutantsCytoplasmic domain sequencesVesicular stomatitis virus glycoproteinVSV G proteinTemperature-sensitive mutantViral G proteinSurface expressionG protein expressionProtein mutantsTransient expressionVirus buddingNonpermissive temperatureDomain sequencesMutantsCell surfaceGlycoprotein mutantsProteinImmunogold labelingSucrose gradientsEfficient assembly