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
1997
Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection
Schnell M, Johnson J, Buonocore L, Rose J. Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection. Cell 1997, 90: 849-857. PMID: 9298897, DOI: 10.1016/s0092-8674(00)80350-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4 AntigensCricetinaeGene DeletionGene Expression Regulation, ViralGlycoproteinsGTP-Binding ProteinsHIV InfectionsHIV-1HumansJurkat CellsKidneyMembrane GlycoproteinsMembrane ProteinsMicroscopy, ImmunoelectronMutagenesisReceptors, CXCR4Receptors, HIVRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsVirus ReplicationConceptsHIV-1-infected cellsHIV-1HIV-1 receptors CD4HIV viral loadHIV-1 infectionInfectious HIV-1Recombinant vesicular stomatitis virusT cell linesHIV infectionViral loadVesicular stomatitis virusTherapeutic valueReceptor CD4Targeted virusInfectionVirusEnvelope proteinCell linesStomatitis virusNormal cellsNovel virusCellsGlycoprotein geneCD4CXCR4
1994
Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA
Rolls M, Webster P, Balba N, Rose J. Novel infectious particles generated by expression of the vesicular stomatitis virus glycoprotein from a self-replicating RNA. Cell 1994, 79: 497-506. PMID: 7954815, DOI: 10.1016/0092-8674(94)90258-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBeta-GalactosidaseCells, CulturedGenetic VectorsHumansMembrane GlycoproteinsModels, GeneticNeutralization TestsParticle SizeRepliconRNA VirusesRNA-Dependent RNA PolymeraseSemliki forest virusSerial PassageSpecies SpecificityTransfectionViral Envelope ProteinsViral Fusion ProteinsVirus ReplicationConceptsVesicular stomatitis virus glycoproteinVSV G proteinSemliki Forest virusStructural proteinsMembrane-enveloped vesiclesRNA repliconsSFV structural proteinsInfectious particlesViral structural proteinsTissue culture cellsVirus glycoproteinAnimal cellsSelf-replicating RNARNA replicaseG proteinsCulture cellsProteinRepliconVirus-like particlesVesiclesVSV serumCellsGlycoproteinExpressionReplicase
1993
Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat.
Buonocore L, Rose J. Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 2695-2699. PMID: 8464877, PMCID: PMC46162, DOI: 10.1073/pnas.90.7.2695.Peer-Reviewed Original ResearchConceptsHuman immunodeficiency virus type 1 productionHIV-1 infectionInfectious HIV-1HIV envelope proteinHuman T cell lineSoluble CD4 proteinT cell linesT cellsHIV-1Viral spreadSyncytium formationInfected cellsViral long terminal repeatCD4CD4 proteinEnvelope proteinIntracellular CD4Intracellular trapsGene therapyLong terminal repeatRetroviral vectorsCellsCell surfaceHIVBlockade
1992
Liposome‐Mediated Transfection
Whitt M, Buonocore L, Rose J. Liposome‐Mediated Transfection. Current Protocols In Immunology 1992, 3: 10.16.1-10.16.4. PMID: 18432679, DOI: 10.1002/0471142735.im1016s03.Peer-Reviewed Original ResearchConceptsDifferent eukaryotic cell typesEukaryotic cell typesTransient expression systemExpression of DNAStable transformationExpression systemCell typesTransfection methodAlternate protocolMonolayer cell culturesDNABasic protocolPlasmid DNACell culturesGenomeCationic lipidsTransfectionExpressionCellsLipids
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 reticulumVirusExpressionCells
1987
An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro.
Rottier P, Florkiewicz R, Shaw A, Rose J. An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro. Journal Of Biological Chemistry 1987, 262: 8889-8895. PMID: 3036834, DOI: 10.1016/s0021-9258(18)47498-4.Peer-Reviewed Original ResearchConceptsSignal sequenceAmino-terminal signal sequenceAmino-terminal presequenceAmino-terminal extensionAmino-terminal coding sequenceVesicular stomatitis virus glycoproteinWild-type efficiencyEukaryotic cellsMembrane insertionSignal peptideCoding sequenceSignal cleavageAmino acidsVirus glycoproteinFull activitySequenceVivoGlycoproteinPresequenceSubsequent transportCleavageGlycosylationInternalizationSuch constructsCellsA critical role for the polarization of membrane recycling in cell motility
Kupfer A, Kronebusch P, Rose J, Singer S. A critical role for the polarization of membrane recycling in cell motility. Cytoskeleton 1987, 8: 182-189. PMID: 2826018, DOI: 10.1002/cm.970080210.Peer-Reviewed Original ResearchConceptsActin cytoskeletonG proteinsMotile cellsCell migrationTemperature-sensitive mutantCell surface appearanceCritical rolePolarized insertionMembrane recyclingMembrane massCell motilityVesicular stomatitis virusCytochalasin DCell surfaceStomatitis virusCytoskeletonLeading edgeCellsMutantsCDNAMigrationInsertionRoleMotilityImmunofluorescence
1986
N protein is the predominant antigen recognized by vesicular stomatitis virus-specific cytotoxic T cells
Puddington L, Bevan M, Rose J, Lefrançois L. N protein is the predominant antigen recognized by vesicular stomatitis virus-specific cytotoxic T cells. Journal Of Virology 1986, 60: 708-717. PMID: 3022003, PMCID: PMC288945, DOI: 10.1128/jvi.60.2.708-717.1986.Peer-Reviewed Original ResearchConceptsN proteinCell linesAnti-vesicular stomatitis virusEL4 cell linePlasma membraneG proteinsVSV genesCompetition assaysProteinNucleocapsid proteinInfected cellsStomatitis virusSodium butyrateGenesEfficient competitorsVSVEL4 cellsCold target competition assaysCellsT cellsCompetition studiesTarget cellsCytotoxic T cellsAssaysImmunoprecipitation
1985
A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface.
Machamer C, Florkiewicz R, Rose J. A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface. Molecular And Cellular Biology 1985, 5: 3074-3083. PMID: 3018499, PMCID: PMC369121, DOI: 10.1128/mcb.5.11.3074.Peer-Reviewed Original ResearchConceptsCell surface expressionG proteinsGlycosylation sitesVesicular stomatitis virus G proteinCell surfaceWild-type proteinVesicular stomatitis virus glycoproteinRole of glycosylationSurface expressionSite-directed mutagenesisVirus G proteinAsparagine-linked glycansIndirect immunofluorescence microscopyIntracellular transportImmunofluorescence microscopyOligosaccharide processingProteinProteolytic breakdownVirus glycoproteinExpressionPalmitic acidCellsMutagenesisOligosaccharidesCDNAA Single N-Linked Oligosaccharide at Either of the Two Normal Sites Is Sufficient for Transport of Vesicular Stomatitis Virus G Protein to the Cell Surface
Machamer C, Florkiewicz R, Rose J. A Single N-Linked Oligosaccharide at Either of the Two Normal Sites Is Sufficient for Transport of Vesicular Stomatitis Virus G Protein to the Cell Surface. Molecular And Cellular Biology 1985, 5: 3074-3083. DOI: 10.1128/mcb.5.11.3074-3083.1985.Peer-Reviewed Original ResearchCell surface expressionG proteinsGlycosylation sitesVesicular stomatitis virus G proteinCell surfaceWild-type proteinVesicular stomatitis virus glycoproteinRole of glycosylationSurface expressionSite-directed mutagenesisVirus G proteinAsparagine-linked glycansIndirect immunofluorescence microscopyIntracellular transportImmunofluorescence microscopyOligosaccharide processingProteinProteolytic breakdownVirus glycoproteinExpressionPalmitic acidCellsMutagenesisOligosaccharidesCDNA
1982
Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells
Rose J, Bergmann J. Expression from cloned cDNA of cell-surface secreted forms of the glycoprotein of vesicular stomatitis virus in eucaryotic cells. Cell 1982, 30: 753-762. PMID: 6291783, DOI: 10.1016/0092-8674(82)90280-x.Peer-Reviewed Original ResearchConceptsG proteinsVesicular stomatitis virusCOS1 cellsCOOH terminusStomatitis virusMouse L cellsSV40 early promoterSV40 late promoterNormal G proteinsTransmembrane domainCDNA clonesEucaryotic cellsLate promoterEarly promoterPlasmid vectorCell typesAmino acidsProteinLipid bilayersL cellsPromoterTerminusG-DNADNACells
1978
Inhibition of translation by poliovirus: inactivation of a specific initiation factor.
Rose J, Trachsel H, Leong K, Baltimore D. Inhibition of translation by poliovirus: inactivation of a specific initiation factor. Proceedings Of The National Academy Of Sciences Of The United States Of America 1978, 75: 2732-2736. PMID: 208073, PMCID: PMC392637, DOI: 10.1073/pnas.75.6.2732.Peer-Reviewed Original ResearchConceptsUninfected cellsHost mRNA translationPoliovirus infectionVSV mRNAsUninfected HeLa cellsInfected cellsSelective inhibitionSlow inactivationMixed extractPoliovirus-induced inhibitionInhibitionMRNACellsPoliovirusLysatesProtein synthesisMRNA translationInitiation factorsInhibition of translationExtractTranslation initiation factor
1976
5'-terminal structure of poliovirus polyribosomal RNA is pUp.
Hewlett M, Rose J, Baltimore D. 5'-terminal structure of poliovirus polyribosomal RNA is pUp. Proceedings Of The National Academy Of Sciences Of The United States Of America 1976, 73: 327-330. PMID: 174102, PMCID: PMC335900, DOI: 10.1073/pnas.73.2.327.Peer-Reviewed Original Research