2001
Mechanisms of Loss of Foreign Gene Expression in Recombinant Vesicular Stomatitis Viruses
Quiñones-Kochs M, Schnell M, Buonocore L, Rose J. Mechanisms of Loss of Foreign Gene Expression in Recombinant Vesicular Stomatitis Viruses. Virology 2001, 287: 427-435. PMID: 11531419, DOI: 10.1006/viro.2001.1058.Peer-Reviewed Original Research
1999
Replication-Competent Rhabdoviruses with Human Immunodeficiency Virus Type 1 Coats and Green Fluorescent Protein: Entry by a pH-Independent Pathway
Boritz E, Gerlach J, Johnson J, Rose J. Replication-Competent Rhabdoviruses with Human Immunodeficiency Virus Type 1 Coats and Green Fluorescent Protein: Entry by a pH-Independent Pathway. Journal Of Virology 1999, 73: 6937-6945. PMID: 10400792, PMCID: PMC112779, DOI: 10.1128/jvi.73.8.6937-6945.1999.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4 AntigensCD4-Positive T-LymphocytesCell LineCricetinaeGreen Fluorescent ProteinsHeLa CellsHIV AntibodiesHIV Envelope Protein gp160HIV-1HumansHydrogen-Ion ConcentrationLigandsLuminescent ProteinsNeutralization TestsReceptors, CCR5Receptors, CXCR4Receptors, HIVRecombination, GeneticVesicular stomatitis Indiana virusVirus ReplicationConceptsVesicular stomatitis virusHuman immunodeficiency virus type 1 (HIV-1) envelope proteinSurrogate virusesRecombinant vesicular stomatitis virusPH-independent pathwayHIV bindingHIV vaccineHIV receptor CD4Coreceptor CXCR4HIV entryCoreceptor specificitySDF-1HIVReceptor CD4Single transmembrane glycoproteinAntibodiesVirusCD4Envelope proteinStomatitis virusCXCR4InfectionTransmembrane glycoproteinGreen fluorescent proteinAdditional recombinants
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
Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection
Schnell M, Johnson J, Buonocore L, Rose J. Construction of a Novel Virus That Targets HIV-1-Infected Cells and Controls HIV-1 Infection. Cell 1997, 90: 849-857. PMID: 9298897, DOI: 10.1016/s0092-8674(00)80350-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4 AntigensCricetinaeGene DeletionGene Expression Regulation, ViralGlycoproteinsGTP-Binding ProteinsHIV InfectionsHIV-1HumansJurkat CellsKidneyMembrane GlycoproteinsMembrane ProteinsMicroscopy, ImmunoelectronMutagenesisReceptors, CXCR4Receptors, HIVRecombinant Fusion ProteinsVesicular stomatitis Indiana virusViral Envelope ProteinsVirus ReplicationConceptsHIV-1-infected cellsHIV-1HIV-1 receptors CD4HIV viral loadHIV-1 infectionInfectious HIV-1Recombinant vesicular stomatitis virusT cell linesHIV infectionViral loadVesicular stomatitis virusTherapeutic valueReceptor CD4Targeted virusInfectionVirusEnvelope proteinCell linesStomatitis virusNormal cellsNovel virusCellsGlycoprotein geneCD4CXCR4
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 ResearchConceptsPrimary 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 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
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 1Degradation
1993
Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat.
Buonocore L, Rose J. Blockade of human immunodeficiency virus type 1 production in CD4+ T cells by an intracellular CD4 expressed under control of the viral long terminal repeat. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 2695-2699. PMID: 8464877, PMCID: PMC46162, DOI: 10.1073/pnas.90.7.2695.Peer-Reviewed Original ResearchConceptsHuman immunodeficiency virus type 1 productionHIV-1 infectionInfectious HIV-1HIV envelope proteinHuman T cell lineSoluble CD4 proteinT cell linesT cellsHIV-1Viral spreadSyncytium formationInfected cellsViral long terminal repeatCD4CD4 proteinEnvelope proteinIntracellular CD4Intracellular trapsGene therapyLong terminal repeatRetroviral vectorsCellsCell surfaceHIVBlockade
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 acidCys394P56lckTransmembraneCD4AcidPalmitateDomainHuman immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum
Crise B, Rose J. Human immunodeficiency virus type 1 glycoprotein precursor retains a CD4-p56lck complex in the endoplasmic reticulum. Journal Of Virology 1992, 66: 2296-2301. PMID: 1548763, PMCID: PMC289024, DOI: 10.1128/jvi.66.4.2296-2301.1992.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumHuman immunodeficiency virusTyrosine kinaseHIV infectionCD4-p56lck complexTransient expression systemGlycoprotein precursorCytoplasmic tyrosine kinaseConfocal immunofluorescence microscopyExpression of CD4HIV-1 gp160Cell surface glycoproteinExpression of gp160Cytoplasmic facePlasma membraneT cell activationExpression systemHeLa cellsImmunofluorescence microscopyCell surfaceImmunodeficiency virusT lymphocytesT cellsLymphocyte killingCD4
1990
CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor
Crise B, Buonocore L, Rose J. CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor. Journal Of Virology 1990, 64: 5585-5593. PMID: 2214026, PMCID: PMC248611, DOI: 10.1128/jvi.64.11.5585-5593.1990.Peer-Reviewed Original ResearchPrevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum
Buonocore L, Rose J. Prevention of HIV-1 glycoprotein transport by soluble CD4 retained in the endoplasmic reticulum. Nature 1990, 345: 625-628. PMID: 2190096, DOI: 10.1038/345625a0.Peer-Reviewed Original ResearchConceptsCD4 moleculeHIV glycoproteinSoluble CD4 moleculesHuman immunodeficiency virusCellular CD4 receptorWild-type CD4Human T cellsInfectious HIVCD4 cellsImmunodeficiency virusSoluble CD4T cellsTherapeutic strategiesCD4 receptorImmunization procedureEnvelope glycoproteinVirus entrySurface expressionCD4HIVIdeal targetEndoplasmic reticulumVirusExpressionCellsShort related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase.
Shaw A, Chalupny J, Whitney J, Hammond C, Amrein K, Kavathas P, Sefton B, Rose J. Short related sequences in the cytoplasmic domains of CD4 and CD8 mediate binding to the amino-terminal domain of the p56lck tyrosine protein kinase. Molecular And Cellular Biology 1990, 10: 1853-1862. PMID: 2109184, PMCID: PMC360530, DOI: 10.1128/mcb.10.5.1853.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, Differentiation, T-LymphocyteBase SequenceCD4 AntigensCD8 AntigensCysteineCytoplasmDNA Mutational AnalysisHumansIn Vitro TechniquesLymphocyte Specific Protein Tyrosine Kinase p56(lck)Molecular Sequence DataProtein BindingProtein-Tyrosine KinasesSignal TransductionStructure-Activity RelationshipConceptsAmino-terminal domainTyrosine protein kinaseCytoplasmic domainProtein kinaseBinding of p56lckCommon sequence motifsRelated amino acid sequencesAmino acid sequenceDisulfide bond formationCD8 alphaAmino acid residuesSequence motifsHybrid proteinCysteine residuesAcid sequenceUnrelated proteinsAlpha proteinRelated sequencesAcid residuesCD4 sequencesP56lckGlycoprotein CD4HeLa cellsProteinKinase
1989
The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain
Shaw A, Amrein K, Hammond C, Stern D, Sefton B, Rose J. The Ick tyrosine protein kinase interacts with the cytoplasmic tail of the CD4 glycoprotein through its unique amino-terminal domain. Cell 1989, 59: 627-636. PMID: 2582490, DOI: 10.1016/0092-8674(89)90008-1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCD4 AntigensCytoplasmHeLa CellsHumansLymphocyte Specific Protein Tyrosine Kinase p56(lck)Macromolecular SubstancesMembrane GlycoproteinsMolecular Sequence DataMutationOligonucleotide ProbesPhosphoproteinsPlasmidsProtein BindingProtein MultimerizationProtein-Tyrosine KinasesT-LymphocytesTransfectionConceptsAmino-terminal domainCytoplasmic domainTyrosine protein kinase p56lckUnique amino-terminal domainT cell-specific proteinsTyrosine protein kinaseSpecific transmembrane proteinsCell-specific proteinsIntracellular tyrosine kinaseAmino-terminal residuesCarboxy-terminal residuesTransmembrane proteinCytoplasmic tailSrc familyProtein kinaseKinase p56lckTyrosine kinaseHeLa cellsCell surfaceProteinDeleted formsSurface glycoproteinP56lckKinaseResidues