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
1992
Human 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
1989
Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum.
Zagouras P, Rose J. Carboxy-terminal SEKDEL sequences retard but do not retain two secretory proteins in the endoplasmic reticulum. Journal Of Cell Biology 1989, 109: 2633-2640. PMID: 2592401, PMCID: PMC2115906, DOI: 10.1083/jcb.109.6.2633.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumSEKDEL sequenceSecretory proteinsSequence Ser-GluAmino acidsMonkey COS cellsOligonucleotide-directed mutagenesisLast amino acidFirst amino acidProtein exitIndirect immunofluorescence microscopyAnimal cellsCOS cellsCOOH terminusAlpha subunitProtein structureGolgi apparatusLys-AspImmunofluorescence microscopyOligosaccharide processingProteinReticulumSEKDELSer-GluSpecific interactions
1987
Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells.
Puddington L, Woodgett C, Rose J. Replacement of the cytoplasmic domain alters sorting of a viral glycoprotein in polarized cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 2756-2760. PMID: 3033661, PMCID: PMC304737, DOI: 10.1073/pnas.84.9.2756.Peer-Reviewed Original ResearchConceptsCytoplasmic domainG proteinsPlasma membraneVesicular stomatitis virusNormal cytoplasmic domainIntegral membrane proteinsPolarized epithelial cellsVSV G proteinApical plasma membraneBasolateral plasma membraneBasolateral membraneCanine kidney cell lineMadin-Darby canine kidney (MDCK) cell lineIndirect immunofluorescence microscopyMembrane proteinsKidney cell lineDomain altersPolarized expressionImmunofluorescence microscopyBasolateral surfaceProteinStomatitis virusCell linesViral glycoproteinsEpithelial cells
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 acidCellsMutagenesisOligosaccharidesCDNAA 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. DOI: 10.1128/mcb.5.11.3074-3083.1985.Peer-Reviewed Original ResearchCell 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 acidCellsMutagenesisOligosaccharidesCDNAA 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. DOI: 10.1128/mcb.5.11.3074-3083.1985.Peer-Reviewed Original ResearchG-proteinCell surface expressionTransport of vesicular stomatitis virus G proteinGlycosylation sitesCell surfaceNonglycosylated G proteinGolgi-like regionWild-type proteinAsparagine-linked glycansVesicular stomatitis virus G proteinSite-directed mutagenesisVesicular stomatitis virus glycoproteinIndirect immunofluorescence microscopyCloned cDNACoding sequenceIntracellular transportOligosaccharide processingSurface expressionTransfected cellsProteolytic breakdownExpression of G-proteinsImmunofluorescence microscopyGlycosylationVirus glycoproteinModified with palmitic acid