2000
Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice
Grigera P, Marzocca M, Capozzo A, Buonocore L, Donis R, Rose J. Presence of bovine viral diarrhea virus (BVDV) E2 glycoprotein in VSV recombinant particles and induction of neutralizing BVDV antibodies in mice. Virus Research 2000, 69: 3-15. PMID: 10989181, DOI: 10.1016/s0168-1702(00)00164-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodies, ViralBase SequenceCattleCell LineChimeraCricetinaeDiarrhea Viruses, Bovine ViralDNA, RecombinantFemaleMembrane GlycoproteinsMiceMice, Inbred BALB CNeutralization TestsRecombinant ProteinsVaccines, SyntheticVesicular stomatitis Indiana virusViral Envelope ProteinsViral VaccinesConceptsBovine viral diarrhea virus (BVDV) E2BALB/c miceRecombinant vesicular stomatitis virusViral-induced diseasesC miceE2 antibodiesBVDV antibodiesVesicular stomatitis virusHigh avidityBVDV E2Recombinant E2Infected cellsDays post inoculationG glycoproteinE2Stomatitis virusMiceAntibodiesImmunofluorescence microscopyPost inoculationRecombinant particlesBHK21 cellsCellsSymptomsInfection
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
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
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 ResearchMeSH KeywordsCD4 AntigensCell LineHIV-1HumansOligopeptidesProtein Sorting SignalsRecombinant ProteinsRepetitive Sequences, Nucleic AcidVirus ReplicationConceptsPrimary 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 inhibitorIsolatesExpressionForeign 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 targetingMembrane 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 proteins
1994
Stimulation 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 1DegradationInteractions 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 virusNucleocapsidsMembrane
1993
Cell 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
1987
Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane.
Scullion B, Hou Y, Puddington L, Rose J, Jacobson K. Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane. Journal Of Cell Biology 1987, 105: 69-75. PMID: 3038931, PMCID: PMC2114925, DOI: 10.1083/jcb.105.1.69.Peer-Reviewed Original ResearchConceptsCytoplasmic domainTransmembrane domainMutant proteinsMembrane proteinsExtracellular domainWild-type G proteinG proteinsMutant G proteinsVesicular stomatitis viral glycoproteinIntegral membrane proteinsEntire cytoplasmic domainLateral mobilitySite-directed mutagenesisEffects of mutationsCOS-1 cellsSlow mutantsFastest mutantPlasma membraneChimeric proteinType G proteinsG cDNAVirus spike glycoproteinPalmitate additionFluorescence recoveryArtificial bilayers