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
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
1996
Expression 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 serumCellsGlycoproteinExpressionReplicaseStimulation 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 1Degradation
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 subunitsProtein
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 virusMutants
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-1.1Mechanism of Membrane Anchoring Affects Polarized Expression of Two Proteins in MDCK Cells
Brown D, Crise B, Rose J. Mechanism of Membrane Anchoring Affects Polarized Expression of Two Proteins in MDCK Cells. Science 1989, 245: 1499-1501. PMID: 2571189, DOI: 10.1126/science.2571189.Peer-Reviewed Original ResearchConceptsMembrane anchorageGPI anchorBasolateral plasma membrane domainsSorting of proteinsPlasma membrane domainsPolarized epithelial cellsClass of proteinsBasolateral surfaceVesicular stomatitis virus glycoproteinMembrane anchoringCytoplasmic domainMembrane domainsMembrane proteinsPolypeptide sequenceTransport signalVSV GPolarized expressionMDCK cellsApical expressionProteinApical surfaceEpithelial cellsVirus glycoproteinPlacental alkaline phosphataseExpressionGlycoprotein 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
1988
Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum.
Shaw A, Rottier P, Rose J. Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 7592-7596. PMID: 2845415, PMCID: PMC282238, DOI: 10.1073/pnas.85.20.7592.Peer-Reviewed Original ResearchConceptsSignal sequenceEndoplasmic reticulumC-terminal transmembraneType II transmembrane proteinInsertion of proteinsCleaved signal sequenceSignal sequence functionN-terminal extensionShort hydrophobic domainVesicular stomatitis virus glycoproteinMembrane anchorMutant proteinsCytoplasmic domainMembrane insertionTransmembrane proteinC-terminusCytoplasmic sideN-terminusBlock cleavageHydrophobic domainCleavage siteHeLa cellsPoint mutationsProteinMicrosomal membranesDifferential 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 surfaceEctodomainProteinFoldingEffects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins.
Guan J, Ruusala A, Cao H, Rose J. Effects of altered cytoplasmic domains on transport of the vesicular stomatitis virus glycoprotein are transferable to other proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. PMID: 2841589, PMCID: PMC363506, DOI: 10.1128/mcb.8.7.2869.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingCytoplasmic sideSecretory proteinsCytoplasmic mutationsG proteinsProteinReticulumDifferent assaysMonomeric structureDetectable effectMutationsSedimentation coefficientRecent studiesEffects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins
Guan J, Ruusala A, Cao H, Rose J. Effects of Altered Cytoplasmic Domains on Transport of the Vesicular Stomatitis Virus Glycoprotein Are Transferable to Other Proteins. Molecular And Cellular Biology 1988, 8: 2869-2874. DOI: 10.1128/mcb.8.7.2869-2874.1988.Peer-Reviewed Original ResearchVesicular stomatitis virus glycoproteinEndoplasmic reticulumCytoplasmic domainVesicular stomatitis virus G proteinHuman chorionic gonadotropinMembrane-anchored formVirus G proteinVirus glycoproteinMutant proteinsProtein foldingChorionic gonadotropinCytoplasmic mutationsCytoplasmic sideSecretory proteinsG proteinsProteinDifferent assaysReticulumCell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit.
Guan J, Cao H, Rose J. Cell-surface expression of a membrane-anchored form of the human chorionic gonadotropin alpha subunit. Journal Of Biological Chemistry 1988, 263: 5306-5313. PMID: 2451667, DOI: 10.1016/s0021-9258(18)60716-1.Peer-Reviewed Original ResearchMeSH KeywordsBiological Transport, ActiveCloning, MolecularDNAElectrophoresis, Polyacrylamide GelFluorescent Antibody TechniqueGene Expression RegulationGlycoprotein Hormones, alpha SubunitGlycoside HydrolasesGlycosylationHexosaminidasesHumansKineticsMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembranesOligosaccharidesPituitary Hormones, AnteriorPlasmidsTunicamycinVesicular stomatitis Indiana virusViral Fusion ProteinsConceptsVesicular stomatitis virus glycoproteinAsparagine-linked glycansAnimal cellsAlpha subunitNovel cell surface proteinCarboxyl-terminal amino acidsGlycosylation inhibitor tunicamycinAbsence of glycosylationMembrane-anchored formCell surface proteinsSecond glycosylation siteHuman chorionic gonadotropin (hCG) alpha-subunitVirus glycoproteinEntire precursorCell surface expressionCytoplasmic domainGonadotropin alpha subunitHybrid proteinPlasma membraneGlycosylation sitesSecretory proteinsCellular membranesConformational changesCell surfaceAmino acidsA 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 linesTerminusGlycoproteinPeptidesMutagenesisCytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane.
Puddington L, Machamer C, Rose J. Cytoplasmic domains of cellular and viral integral membrane proteins substitute for the cytoplasmic domain of the vesicular stomatitis virus glycoprotein in transport to the plasma membrane. Journal Of Cell Biology 1986, 102: 2147-2157. PMID: 3011809, PMCID: PMC2114239, DOI: 10.1083/jcb.102.6.2147.Peer-Reviewed Original ResearchMeSH KeywordsB-LymphocytesBiological Transport, ActiveCell LineCell MembraneCoronaviridaeCytoplasmGenes, ViralHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralHumansImmunoglobulin mu-ChainsMembrane GlycoproteinsMembrane ProteinsOligonucleotidesTransfectionVesicular stomatitis Indiana virusViral Envelope ProteinsViral ProteinsConceptsNormal cytoplasmic domainIntegral membrane proteinsCytoplasmic domainVesicular stomatitis virus glycoproteinG proteinsPlasma membraneHybrid proteinMembrane proteinsCellular integral membrane proteinsViral integral membrane proteinsB cell line WEHI-231Wild-type G proteinCell line WEHI-231Amino acid sequenceRate of transportVirus glycoproteinEukaryotic cellsTransmembrane domainChimeric cDNAHybrid geneWEHI-231Acid sequenceType G proteinsHeavy chain moleculesGolgi complex
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 acidCellsMutagenesisOligosaccharidesCDNA