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
1996
Replication of Primary HIV-1 Isolates Is Inhibited in PM1 Cells Expressing sCD4-KDEL
Degar S, Johnson J, Boritz E, Rose J. Replication of Primary HIV-1 Isolates Is Inhibited in PM1 Cells Expressing sCD4-KDEL. Virology 1996, 226: 424-429. PMID: 8955064, DOI: 10.1006/viro.1996.0672.Peer-Reviewed Original ResearchConceptsPrimary HIV-1 isolatesPrimary HIV-1HIV-1 isolatesPrimary isolatesHIV-1HIV-1-infected individualsCell linesSoluble CD4 moleculesHIV-1 spreadHIV-1 replicationGene therapy-based approachesHIV-1 LTRHIV-1MN strainTreatment of AIDST cell linesCell culture supernatantsCD4 moleculePM1 cellsVirus presentPM1 cell linesPrototype strainCulture supernatantsPotent inhibitorIsolatesExpression
1987
Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells.
Puddington L, Woodgett C, Rose J. Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 2756-2760. PMID: 3033661, PMCID: PMC304737, DOI: 10.1073/pnas.84.9.2756.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsPlasma membraneVesicular stomatitis virusNormal cytoplasmic domainIntegral membrane proteinsPolarized epithelial cellsVSV G proteinApical plasma membraneBasolateral plasma membraneBasolateral membraneCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineIndirect immunofluorescence microscopyMembrane proteinsKidney cell lineDomain altersPolarized expressionImmunofluorescence microscopyBasolateral surfaceProteinStomatitis virusCell linesViral glycoproteinsEpithelial cells
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 cellsAssaysImmunoprecipitationAmino-terminal mutation of the vesicular stomatitis virus glycoprotein does not affect its fusion activity
Woodgett C, Rose J. Amino-terminal mutation of the vesicular stomatitis virus glycoprotein does not affect its fusion activity. Journal Of Virology 1986, 59: 486-489. PMID: 3016308, PMCID: PMC253100, DOI: 10.1128/jvi.59.2.486-489.1986.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinAmino acid changesG proteinsFusion activityAmino terminusWild-type G proteinAcid changesAmino-terminal mutationsSingle amino acid changeMonkey fibroblast cell lineSame amino acid changeOligonucleotide-directed mutagenesisPH-dependent fusion activityVirus glycoproteinPH-dependent hemolytic activityMutant proteinsHemolytic activityFibroblast cell lineSynthetic peptidesProteinCell linesTerminusGlycoproteinPeptidesMutagenesis
1983
Isolation of stable mouse cell lines that express cell surface and secreted forms of the vesicular stomatitis virus glycoprotein.
Florkiewicz R, Smith A, Bergmann J, Rose J. Isolation of stable mouse cell lines that express cell surface and secreted forms of the vesicular stomatitis virus glycoprotein. Journal Of Cell Biology 1983, 97: 1381-1388. PMID: 6415065, PMCID: PMC2112694, DOI: 10.1083/jcb.97.5.1381.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinMouse cell linesG proteinsNormal G proteinsStable mouse cell linesEndoplasmic reticulumCell linesTg proteinRough endoplasmic reticulumVesicular stomatitis virus G proteinCell surfaceVirus G proteinBovine papilloma virusVirus glycoproteinComplex oligosaccharidesAnchor sequenceLevel of expressionPSV2 vectorCDNA encodingAnchorless proteinAberrant splicingDNA fragmentsGolgi apparatusMRNA sequencesRate-limiting step