2001
Vesicular Stomatitis Virus Glycoprotein Containing the Entire Green Fluorescent Protein on Its Cytoplasmic Domain Is Incorporated Efficiently into Virus Particles
Dalton K, Rose J. Vesicular Stomatitis Virus Glycoprotein Containing the Entire Green Fluorescent Protein on Its Cytoplasmic Domain Is Incorporated Efficiently into Virus Particles. Virology 2001, 279: 414-421. PMID: 11162797, DOI: 10.1006/viro.2000.0736.Peer-Reviewed Original ResearchConceptsLarge cytoplasmic domainCytoplasmic domainVSV G proteinVesicular stomatitis virusGreen fluorescent proteinG proteinsGFP proteinWild-type G proteinFluorescent proteinShort cytoplasmic domainVesicular stomatitis virus glycoproteinStrong selectionVirus particlesExtra genesHeterotrimeric proteinGFP geneProtein sequencesWild-type virusFluorescent virus particlesStop codonVirus assemblyInfectious cloneGenesViral membraneAmino acids
2000
Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope
Haglund K, Forman J, Kräusslich H, Rose J. Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope. Virology 2000, 268: 112-121. PMID: 10683333, DOI: 10.1006/viro.1999.0120.Peer-Reviewed Original ResearchMeSH KeywordsAIDS VaccinesAnimalsCell LineDNA, RecombinantGene Products, gagGenetic VectorsHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicroscopy, ElectronPlasmidsProtein PrecursorsRecombinant Fusion ProteinsVaccines, AttenuatedVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsHIV virus-like particlesVirus-like particlesEnv proteinHIV-1HIV-1 envelope proteinAntibody-mediated immunityHigh-level productionRecombinant vesicular stomatitis virusVSV particlesHIV Env proteinEnvelope proteinEffective vaccine vectorHIV-like particlesProtein precursorHIV envelopeHigh-level expression vectorVaccine vectorHIV recombinantsVesicular stomatitis virusVirus titersVirus recombinantsVSV G proteinG proteinsStomatitis virusExpression vector
1999
Attenuated Vesicular Stomatitis Viruses as Vaccine Vectors
Roberts A, Buonocore L, Price R, Forman J, Rose J. Attenuated Vesicular Stomatitis Viruses as Vaccine Vectors. Journal Of Virology 1999, 73: 3723-3732. PMID: 10196265, PMCID: PMC104148, DOI: 10.1128/jvi.73.5.3723-3732.1999.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell LineCricetinaeFemaleGene ExpressionGenetic VectorsHemagglutinin Glycoproteins, Influenza VirusInfluenza VaccinesMembrane GlycoproteinsMiceMice, Inbred BALB COrthomyxoviridae InfectionsRecombination, GeneticTime FactorsVaccines, AttenuatedVaccines, SyntheticVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsVesicular stomatitis virusLethal influenza virus challengeComplete protectionInfluenza virus challengeRecombinant vesicular stomatitis virusSingle intranasal vaccinationInfluenza virus HAStomatitis virusIntranasal vaccinationLethal challengeIntranasal administrationVirus challengeMouse modelVaccine vectorVSV vectorsVirus HAInfluenza virusHemagglutinin proteinInfluenza virus hemagglutinin (HA) proteinG proteinsPathogenesisVirus hemagglutinin proteinVirusPresent studyVaccination
1998
Requirement 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
1997
High-efficiency incorporation of functional influenza virus glycoproteins into recombinant vesicular stomatitis viruses
Kretzschmar E, Buonocore L, Schnell M, Rose J. High-efficiency incorporation of functional influenza virus glycoproteins into recombinant vesicular stomatitis viruses. Journal Of Virology 1997, 71: 5982-5989. PMID: 9223488, PMCID: PMC191854, DOI: 10.1128/jvi.71.8.5982-5989.1997.Peer-Reviewed Original ResearchConceptsVSV G proteinVesicular stomatitis virusG proteinsForeign membrane proteinsForeign proteinsVirus membrane glycoproteinsVSV particlesVSV G geneNA proteinsStomatitis virusGene orderExtra genesVSV transcriptionMembrane proteinsRecombinant vesicular stomatitis virusSite upstreamVSV virionsVSV membraneHA proteinInfluenza virus proteinsInfluenza virus glycoproteinsGlycoprotein geneGlycoprotein CD4Membrane glycoproteinsViral genome
1996
Foreign glycoproteins expressed from recombinant vesicular stomatitis viruses are incorporated efficiently into virus particles.
Schnell M, Buonocore L, Kretzschmar E, Johnson E, Rose J. Foreign glycoproteins expressed from recombinant vesicular stomatitis viruses are incorporated efficiently into virus particles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 11359-11365. PMID: 8876140, PMCID: PMC38062, DOI: 10.1073/pnas.93.21.11359.Peer-Reviewed Original ResearchConceptsVSV G proteinDifferent membrane proteinsVesicular stomatitis virusG proteinsMembrane proteinsMembrane protein purificationEctodomain of CD4Virus particlesStomatitis virusWild-type virionsVirus fusion proteinExtra genesHybrid proteinCytoplasmic tailHelical nucleocapsidMammalian cellsRecombinant vesicular stomatitis virusVSV G.Fusion proteinMeasles virus fusion proteinSoluble proteinMembrane envelopeCell surfaceProtein purificationViral targetingExpression of Additional Genes in a Vector Derived from a Minimal RNA Virus
ROLLS M, HAGLUND K, ROSE J. Expression of Additional Genes in a Vector Derived from a Minimal RNA Virus. Virology 1996, 218: 406-411. PMID: 8610469, DOI: 10.1006/viro.1996.0211.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCapsidCD4 AntigensCell LineChloramphenicol O-AcetyltransferaseCloning, MolecularCricetinaeGene ExpressionGenetic VectorsMembrane GlycoproteinsMolecular Sequence DataPromoter Regions, GeneticRecombinant Fusion ProteinsRNA, ViralSemliki forest virusVesicular stomatitis Indiana virusViral Core ProteinsViral Envelope ProteinsConceptsVSV G proteinG proteinsVSV G geneVesicular stomatitis virus glycoproteinTotal cell proteinMembrane fusion activityViral structural proteinsHost protein synthesisTissue culture cellsUnselected genesMultiple cloning siteInfectious particlesAdditional genesForeign genesPlasma membraneG RNADifferent proteinsStructural proteinsMajor proteinsRNA repliconsCell proteinsFusion activityRNA virusesProtein synthesisGenes
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 serumCellsGlycoproteinExpressionReplicaseMutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity
Owens R, Burke C, Rose J. Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotein that affect fusion activity. Journal Of Virology 1994, 68: 570-574. PMID: 8254774, PMCID: PMC236324, DOI: 10.1128/jvi.68.1.570-574.1994.Peer-Reviewed Original ResearchConceptsTransmembrane domainFusion activityVesicular stomatitis virus G proteinMembrane-spanning domainsCell surfaceSpecific amino acid sequencesAmino acid sequenceMembrane fusion activityAmino acid residuesMembrane fusion processCytoplasmic tail domainVirus G proteinCytoplasmic domainMutagenic analysisAcid sequenceChimeric proteinBasic residuesProtein ectodomainAcid residuesG proteinsHeLa cellsVirus envelope glycoproteinLipid bilayersProteinGp41 transmembrane
1993
Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface
Zagouras P, Rose J. Dynamic equilibrium between vesicular stomatitis virus glycoprotein monomers and trimers in the Golgi and at the cell surface. Journal Of Virology 1993, 67: 7533-7538. PMID: 8230472, PMCID: PMC238219, DOI: 10.1128/jvi.67.12.7533-7538.1993.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, ViralAntibody SpecificityBiological TransportBrefeldin ACell CompartmentationCell MembraneCells, CulturedCricetinaeCyclopentanesGolgi ApparatusHexosaminidasesMembrane GlycoproteinsMutationPostural BalanceProtein ConformationProtein Processing, Post-TranslationalVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsEndoplasmic reticulumHeterotrimer formationG proteinsMutant G proteinsG protein trimersVesicular stomatitis virus glycoproteinG protein subunitsVSV G proteinProtein moleculesG protein moleculesWild-type trimersMutant proteinsCytoplasmic domainCellular compartmentsCoexpression experimentsGlycoprotein monomersLonger chase periodsPlasma membraneProtein subunitsMu proteinProtein trimerForms trimersCell surfaceMonomeric subunitsProteinCytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus
Owens R, Rose J. Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus. Journal Of Virology 1993, 67: 360-365. PMID: 8093220, PMCID: PMC237371, DOI: 10.1128/jvi.67.1.360-365.1993.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCD4-Positive T-LymphocytesCell FusionFluorescent Antibody TechniqueGene Products, envHIV Envelope Protein gp120HIV Envelope Protein gp41HIV-1Membrane GlycoproteinsMolecular Sequence DataRecombinant Fusion ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsHIV-1 envelope proteinEnvelope proteinAnti-HIV-1 seraHuman immunodeficiency virus type 1 (HIV-1) envelope proteinG proteinsHIV-1 entryVesicular stomatitis virus particlesHIV-1Vesicular stomatitis virusEnvelope glycoproteinWild-type G proteinStomatitis virusVSV particlesVSV G proteinVirus particlesTemperature-sensitive mutantPseudotypesSimultaneous expressionTransmembrane domainCytoplasmic domainCytoplasmic tailDefective transportVSV
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 crosslinkingFatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions
Whitt M, Rose J. Fatty acid acylation is not required for membrane fusion activity or glycoprotein assembly into VSV virions. Virology 1991, 185: 875-878. PMID: 1660205, DOI: 10.1016/0042-6822(91)90563-q.Peer-Reviewed Original ResearchConceptsFatty acid acylationVSV G proteinMembrane fusion activityVesicular stomatitis virusG proteinsWild-type G proteinFusion activityWild-type proteinTemperature-sensitive mutantCytoplasmic domainTransient expressionPresence of palmitateVSV virionsIndiana serotypeHeLa cellsExpression of CSProteinStomatitis virusLife cycleSyncytium formationExpressionMutantsAcylationVirionsVirusDissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum
Zagouras P, Ruusala A, Rose J. Dissociation and reassociation of oligomeric viral glycoprotein subunits in the endoplasmic reticulum. Journal Of Virology 1991, 65: 1976-1984. PMID: 1848313, PMCID: PMC240033, DOI: 10.1128/jvi.65.4.1976-1984.1991.Peer-Reviewed Original ResearchConceptsWild-type ratesEndoplasmic reticulumMutant subunitsG proteinsCell surfaceG protein trimersWild-type subunitsFormation of heterotrimersWild-type moleculeWild-type trimersMutant proteinsRetention signalProtein trimerHeterotrimerSubunitsGlycoprotein subunitsProteinReticulumGlycoprotein formTrimerTransport blockHomotrimersReassociation
1990
A fusion-defective mutant of the vesicular stomatitis virus glycoprotein
Whitt M, Zagouras P, Crise B, Rose J. A fusion-defective mutant of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1990, 64: 4907-4913. PMID: 2168975, PMCID: PMC247981, DOI: 10.1128/jvi.64.10.4907-4913.1990.Peer-Reviewed Original ResearchConceptsWild-type G proteinG proteinsMutant proteinsFusion activityMutant G proteinsFusion-defective mutantsAmino acids 117Vesicular stomatitis virus glycoproteinFormation of heterotrimersUncharged amino acidsTemperature-sensitive mutantNew glycosylation siteMutant glycoproteinsVesicular stomatitis virusGlycosylation sitesMembrane fusionRescue of virusVSV virionsExtracellular domainAmino acidsCell surfaceProteinVSV serotypesStomatitis virusMutantsHeavy 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-1.1Glycoprotein 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 assemblyA single-amino-acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein
Pitta A, Rose J, Machamer C. A single-amino-acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein. Journal Of Virology 1989, 63: 3801-3809. PMID: 2760984, PMCID: PMC250973, DOI: 10.1128/jvi.63.9.3801-3809.1989.Peer-Reviewed Original Research
1988
Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein.
Doms R, Ruusala A, Machamer C, Helenius J, Helenius A, Rose J. Differential effects of mutations in three domains on folding, quaternary structure, and intracellular transport of vesicular stomatitis virus G protein. Journal Of Cell Biology 1988, 107: 89-99. PMID: 2839523, PMCID: PMC2115181, DOI: 10.1083/jcb.107.1.89.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalAntibody SpecificityBiological TransportCell LineCentrifugation, Density GradientElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumGlycosylationImmunoassayKineticsMacromolecular SubstancesMembrane GlycoproteinsMutationProtein ConformationTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral Matrix ProteinsConceptsG proteinsMutant proteinsCytoplasmic domainMutant G proteinsVesicular stomatitis virus G proteinIntegral membrane proteinsWild-type proteinTrimer formationVesicular stomatitis virus glycoproteinVirus G proteinAltered glycosylation patternConformation-specific antibodiesTail mutationsMembrane proteinsMin of synthesisOligomeric assembliesQuaternary structureMature formEndoplasmic reticulumInitial foldingGlycosylation patternsCell surfaceEctodomainProteinFolding