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
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
1991
Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein
Whitt M, Buonocor L, Prehaud C, Rose J. Membrane fusion activity, oligomerization, and assembly of the rabies virus glycoprotein. Virology 1991, 185: 681-688. PMID: 1660200, DOI: 10.1016/0042-6822(91)90539-n.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, ViralBase SequenceCell LineCentrifugation, Density GradientCricetinaeFlow CytometryGenetic Complementation TestGlycoproteinsHumansHydrogen-Ion ConcentrationKineticsMacromolecular SubstancesMembrane FusionMembrane GlycoproteinsMiceMolecular Sequence DataPlasmidsRabies virusRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsVSV G proteinG protein trimersMembrane fusion activityVirus G proteinG proteinsRabies G proteinFusion activityHybrid proteinProtein trimerVesicular stomatitis virus G proteinVirus glycoproteinRabies virus glycoproteinCytoplasmic domainMembrane fusionExtracellular domainHeLa cellsRabies virus G proteinCell surfaceProteinVSV particlesSucrose gradientsVSV infectivityGlycoproteinSpike glycoproteinChemical crosslinking
1990
Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein.
Machamer C, Doms R, Bole D, Helenius A, Rose J. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. Journal Of Biological Chemistry 1990, 265: 6879-6883. PMID: 2157712, DOI: 10.1016/s0021-9258(19)39231-2.Peer-Reviewed Original ResearchConceptsMutant G proteinsHeavy chain binding proteinG proteinsEndoplasmic reticulumWild-type G proteinBinding proteinVesicular stomatitis virus G proteinPlasma membrane glycoproteinsVirus G proteinAnti-BiP antibodiesDisulfide-bonded formIntrachain disulfide bondsVesicular stomatitis virusMembrane glycoproteinsDisulfide bondsBiPProteinStomatitis virusReticulumImmunoprecipitationGlycoprotein
1989
Oligomerization 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-1.1
1988
A membrane-anchored form but not the secretory form of human chorionic gonadotropin-alpha chain acquires polylactosaminoglycan.
Fukuda M, Guan J, Rose J. A membrane-anchored form but not the secretory form of human chorionic gonadotropin-alpha chain acquires polylactosaminoglycan. Journal Of Biological Chemistry 1988, 263: 5314-5318. PMID: 2451668, DOI: 10.1016/s0021-9258(18)60717-3.Peer-Reviewed Original ResearchConceptsMembrane-anchored formHuman chorionic gonadotropin (hCG) alpha-subunitMembrane anchoringGonadotropin alpha subunitSecretory formVesicular stomatitis virus glycoproteinMonkey COS-1 cellsCOS-1 cellsMembrane-bound formCytoplasmic domainMembrane proteinsSecretory proteinsComplex-type oligosaccharidesSecretory glycoproteinsProteinDNAVirus glycoproteinSubunitsPolylactosaminoglycansCarbohydrate structuresGlycoproteinGlycansAnchoringAsnEnzyme
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 constructsCells
1986
Amino-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
1984
The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition.
Rose J, Adams G, Gallione C. The presence of cysteine in the cytoplasmic domain of the vesicular stomatitis virus glycoprotein is required for palmitate addition. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 2050-2054. PMID: 6326102, PMCID: PMC345434, DOI: 10.1073/pnas.81.7.2050.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsVesicular stomatitis virusVesicular stomatitis virus glycoproteinVSV G proteinCarboxyl-terminal sideAmino acid residuesEukaryotic cellsTransmembrane domainCDNA clonesGene resultsAcid residuesCellular membranesPalmitate additionTransmembrane glycoproteinCellular glycoproteinsCell surfaceAmino acidsProteinStomatitis virusCysteineVirus glycoproteinPresence of cysteineFatty acidsGlycoprotein