1998
A Plasma Membrane Localization Signal in the HIV-1 Envelope Cytoplasmic Domain Prevents Localization at Sites of Vesicular Stomatitis Virus Budding and Incorporation into VSV Virions
Johnson J, Rodgers W, Rose J. A Plasma Membrane Localization Signal in the HIV-1 Envelope Cytoplasmic Domain Prevents Localization at Sites of Vesicular Stomatitis Virus Budding and Incorporation into VSV Virions. Virology 1998, 251: 244-252. PMID: 9837788, DOI: 10.1006/viro.1998.9429.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell MembraneCells, CulturedCricetinaeCytoplasmGene Products, envHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicroscopy, ConfocalMolecular Sequence DataProtein Sorting SignalsRecombinant ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsVSV virionsMembrane-proximal amino acidsMembrane localization signalAmino acidsVesicular stomatitis virus (VSV) virionsLocalization signalMembrane domainsG-tailsCytoplasmic tailVirus buddingPrevents localizationVirus virionsMutantsVSV proteinsProteinConfocal microscopyVSV recombinantsEnvelope proteinVSV glycoproteinHuman Immunodeficiency Virus Type 1 EnvVirionsHIV-1 envelope proteinEnv proteinTailHybrids
1996
Membrane Association of Influenza Virus Matrix Protein Does Not Require Specific Hydrophobic Domains or the Viral Glycoproteins
KRETZSCHMAR E, BUI M, ROSE J. Membrane Association of Influenza Virus Matrix Protein Does Not Require Specific Hydrophobic Domains or the Viral Glycoproteins. Virology 1996, 220: 37-45. PMID: 8659126, DOI: 10.1006/viro.1996.0283.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBinding SitesCell LineCell MembraneChick EmbryoDogsHeLa CellsHemagglutinin Glycoproteins, Influenza VirusHemagglutinins, ViralHumansInfluenza A virusMolecular Sequence DataMutagenesis, Site-DirectedNeuraminidaseOligodeoxyribonucleotidesRecombinant ProteinsViral Matrix ProteinsConceptsMembrane associationSpecific hydrophobic domainsM1 proteinMatrix proteinsHydrophobic domainInfluenza virus matrix proteinVirus matrix proteinInteraction of M1Viral glycoproteinsMajor structural componentRibonucleocapsid coreCytoplasmic tailIntegral proteinsMembrane proteinsMembrane bindingSubcellular fractionationMembrane envelopeCellular membranesHeLa cellsViral proteinsHydrophobic regionProteinIsolated membranesMembraneInfluenza proteinsCharacterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗)
Turi T, Mueller U, Sazer S, Rose J. Characterization of a Nuclear Protein Conferring Brefeldin A Resistance in Schizosaccharomyces pombe (∗). Journal Of Biological Chemistry 1996, 271: 9166-9171. PMID: 8621569, DOI: 10.1074/jbc.271.15.9166.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntifungal AgentsBase SequenceBrefeldin ACell CompartmentationConsensus SequenceCyclopentanesDNA PrimersDrug Resistance, MicrobialFungal ProteinsGenes, FungalGolgi ApparatusGTP-Binding ProteinsMolecular Sequence DataNuclear ProteinsPhosphoproteinsRan GTP-Binding ProteinRestriction MappingSchizosaccharomycesSequence AlignmentSequence Homology, Amino AcidConceptsNuclear pore complexWild type SchizosaccharomycesPore complexS. pombeSchizosaccharomyces pombeProtein RanBP1Essential proteinsGolgi complexEndoplasmic reticulumProtein secretionPeptide motifsMultiple copiesNovel mechanismGenesProteinPombeA ResistanceBrefeldinDrug resistanceSchizosaccharomycesYrb1RanBP1HomologyComplexesReticulumNormal Replication of Vesicular Stomatitis Virus without C Proteins
KRETZSCHMAR E, PELUSO R, SCHNELL M, WHITT M, ROSE J. Normal Replication of Vesicular Stomatitis Virus without C Proteins. Virology 1996, 216: 309-316. PMID: 8607260, DOI: 10.1006/viro.1996.0066.Peer-Reviewed Original ResearchConceptsP geneWild-type virusNormal replicationSmall basic proteinP protein sequenceSingle base changeNew Jersey serotypeWild-type virus particlesInsect vectorsVesicular stomatitis virusC proteinStop codonViral mRNAsVSV growthInfectious cloneBase changesMutant virusProteinGenesStomatitis virusViral pathogenesisBasic proteinM proteinVirus particlesTissue culture
1995
Replication and amplification of novel vesicular stomatitis virus minigenomes encoding viral structural proteins
Stillman E, Rose J, Whitt M. Replication and amplification of novel vesicular stomatitis virus minigenomes encoding viral structural proteins. Journal Of Virology 1995, 69: 2946-2953. PMID: 7707520, PMCID: PMC188993, DOI: 10.1128/jvi.69.5.2946-2953.1995.Peer-Reviewed Original ResearchConceptsVesicular stomatitis virusViral structural proteinsStructural proteinsMatrix protein geneFunctional viral proteinsM proteinNorthern blot analysisEncoded proteinsInfectious particlesTranscriptional eventsFunctional mRNAProtein geneL proteinLeader regionMinigenome RNAVSV genomeIndiana serotypePolymerase proteinOwn propagationGlycoprotein geneVSV proteinsViral proteinsProteinNucleocapsid proteinMinigenome
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 1DegradationSignals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction.
Rodgers W, Crise B, Rose J. Signals determining protein tyrosine kinase and glycosyl-phosphatidylinositol-anchored protein targeting to a glycolipid-enriched membrane fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. PMID: 8035816, PMCID: PMC359057, DOI: 10.1128/mcb.14.8.5384.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell CompartmentationDNA PrimersGlycolipidsGlycosylphosphatidylinositolsHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataMutagenesis, Site-DirectedMyristatesPalmitatesProtein-Tyrosine KinasesProteinsStructure-Activity RelationshipConceptsProtein tyrosine kinasesCertain protein tyrosine kinasesTyrosine kinaseMembrane fractionSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorGlycosyl phosphatidylinositolKinaseP56lckCell typesHeLa cellsMDCK cellsGPIProteinGentle disruptionSignals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction
Rodgers W, Crise B, Rose J. Signals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. DOI: 10.1128/mcb.14.8.5384-5391.1994.Peer-Reviewed Original ResearchProtein tyrosine kinasesCertain protein tyrosine kinasesP56 lckTyrosine kinaseMembrane fractionGlycosyl phosphatidylinositolSrc family protein tyrosine kinasesFamily protein tyrosine kinasesAnalysis of mutantsN-terminal myristateCy-3Glycolipid-enriched membranesAssociation of p56lckCys-5Membrane domainsMembrane proteinsAnchored proteinsGPI anchorKinaseCell typesHeLa cellsLckMDCK cellsGPIProteinSignals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction
Rodgers W, Crise B, Rose J. Signals Determining Protein Tyrosine Kinase and Glycosyl-Phosphatidylinositol-Anchored Protein Targeting to a Glycolipid-Enriched Membrane Fraction. Molecular And Cellular Biology 1994, 14: 5384-5391. DOI: 10.1128/mcb.14.8.5384-5391.1994.Peer-Reviewed Original ResearchGPI-anchored proteinsProtein tyrosine kinasesGlycolipid-enriched membraneP56 LckTyrosine kinaseMembrane fractionCys-3Glycosyl-phosphatidylinositol (GPI)-anchored membrane proteinsGlycolipid-enriched membrane fractionCys-5Src family protein tyrosine kinasesTriton X-100-insolubleAnalysis of mutantsGlycosyl-phosphatidylinositol-anchored proteinsN-terminal myristateAssociation of p56lckGPI anchorTransmembrane signalingMembrane proteinsMembrane domainsHeLa cellsKinaseLckProteinTarget signalInteractions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids
Chong L, Rose J. Interactions of normal and mutant vesicular stomatitis virus matrix proteins with the plasma membrane and nucleocapsids. Journal Of Virology 1994, 68: 441-447. PMID: 8254754, PMCID: PMC236304, DOI: 10.1128/jvi.68.1.441-447.1994.Peer-Reviewed Original ResearchConceptsMembrane associationPlasma membraneAmino-terminal basic domainVesicular stomatitis virusWild-type M proteinCellular membranesMatrix proteinsVesicular stomatitis virus matrix proteinM proteinStable membrane associationTruncated M proteinsVirus matrix proteinVSV nucleocapsidsBasic domainAmino terminusNucleocapsid bindingNucleocapsid interactionMembrane fractionVSV proteinsAmino acidsMembrane specificityProteinStomatitis virusNucleocapsidsMembraneMutations 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 subunitsProteinFolding and Assembly of Viral Membrane Proteins
Doms R, Lamb R, Rose J, Helenius A. Folding and Assembly of Viral Membrane Proteins. Virology 1993, 193: 545-562. PMID: 8460475, DOI: 10.1006/viro.1993.1164.Peer-Reviewed Original ResearchConceptsViral membrane proteinsQuality control mechanismsMolecular chaperonesGRP78-BiPMembrane proteinsER molecular chaperonesEffects of mutationsMisfolded proteinsProtein transportConformational maturationMisfolded moleculesProtein foldingEnergy-driven processChaperonesProtein structureMolecular mechanismsER environmentGRP78 synthesisExogenous proteinsNascent moleculesProteinDirect roleStructural variabilityControl mechanismsExperimental strategiesCell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease
Cattaneo R, Rose J. Cell fusion by the envelope glycoproteins of persistent measles viruses which caused lethal human brain disease. Journal Of Virology 1993, 67: 1493-1502. PMID: 8437226, PMCID: PMC237519, DOI: 10.1128/jvi.67.3.1493-1502.1993.Peer-Reviewed Original ResearchMeSH KeywordsAutopsyBacteriophage T7Biological TransportBrain DiseasesCell FusionCell LineCloning, MolecularDNA, ViralGlycosylationHeLa CellsHemagglutinins, ViralHumansMeaslesMeasles virusOligosaccharidesPromoter Regions, GeneticProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsRNA, ViralViral Envelope ProteinsViral Fusion ProteinsViral InterferenceViral Matrix ProteinsVirulenceConceptsIntegral membrane proteinsH proteinCell fusionMembrane proteinsIntracellular domainViral buddingM proteinHS-protein interactionsF protein functionProtein interactionsMV genesIntracellular transportFusion proteinOligosaccharide modificationViral envelope proteinsMatrix proteinsHuman brain diseasesProteinMeasles virusReduced expressionEnvelope proteinPersistent measles virusBuddingSyncytium formationDisease developmentMembrane association of functional vesicular stomatitis virus matrix protein in vivo
Chong L, Rose J. Membrane association of functional vesicular stomatitis virus matrix protein in vivo. Journal Of Virology 1993, 67: 407-414. PMID: 8380086, PMCID: PMC237377, DOI: 10.1128/jvi.67.1.407-414.1993.Peer-Reviewed Original ResearchMeSH KeywordsCell MembraneCytosolHeLa CellsHumansMacromolecular SubstancesMembrane ProteinsModels, BiologicalOctoxynolPolyethylene GlycolsProtein ConformationRecombinant ProteinsRibonucleoproteinsSolubilitySubcellular FractionsVesicular stomatitis Indiana virusViral Core ProteinsViral Matrix ProteinsConceptsVesicular stomatitis virusRNP coresMatrix proteinsVesicular stomatitis virus matrix proteinM proteinVirus matrix proteinSoluble M proteinMajor structural componentRibonucleocapsid coreMembrane associationMembrane proteinsM protein moleculeVirus buddingSubcellular fractionationCellular membranesMembrane envelopeHeLa cellsVSV proteinsViral proteinsDetergent Triton XProteinProtein moleculesConformational differencesStomatitis virusMembrane
1992
Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor.
Crise B, Rose J. Identification of palmitoylation sites on CD4, the human immunodeficiency virus receptor. Journal Of Biological Chemistry 1992, 267: 13593-13597. PMID: 1618861, DOI: 10.1016/s0021-9258(18)42253-3.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBinding of p56lckHuman immunodeficiency virus receptorCell surface glycoprotein CD4Palmitoylation sitesCysteine residuesThioester linkageGlycoprotein CD4HeLa cellsCell surfaceVirus receptorProteinFatty acidsMutationsCysteineExpression of CD4Cys397Palmitic acidCys394P56lckTransmembraneCD4AcidPalmitateDomainSorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
Brown D, Rose J. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68: 533-544. PMID: 1531449, DOI: 10.1016/0092-8674(92)90189-j.Peer-Reviewed Original ResearchConceptsBasolateral marker proteinsCertain membrane proteinsApical cell surfaceDetergent-insoluble formGlycosylphosphatidyl inositol (GPI) anchorMembrane subdomainsMembrane proteinsIntracellular associationGolgi complexMicrodomains formGolgi apparatusInositol anchorMarker proteinsCell surfaceProteinApical surfaceEpithelial cellsGPIGlycosphingolipidsComplexesVesiclesLysatesGlycolipidsSortingMembrane
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 formationExpressionMutantsAcylationVirionsVirus