2021
Fitness selection of hyperfusogenic measles virus F proteins associated with neuropathogenic phenotypes
Ikegame S, Hashiguchi T, Hung C, Dobrindt K, Brennand K, Takeda M, Lee B. Fitness selection of hyperfusogenic measles virus F proteins associated with neuropathogenic phenotypes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2026027118. PMID: 33903248, PMCID: PMC8106313, DOI: 10.1073/pnas.2026027118.Peer-Reviewed Original ResearchConceptsF mutantsMeasles inclusion body encephalitisBSR-T7 cellsMeasles virus F proteinReceptor-binding proteinVirus F proteinGenomic contextFitness advantageWild-type MeVRegulatory domainHyperfusogenic phenotypePrimary human neuronsMutant libraryPoint mutantsMutantsFitness selectionMeV receptorsF phenotypeInclusion body encephalitisNeuropathogenic phenotypeFitness landscapeChronic latent infectionFusion geneF proteinHuman neurons
2015
Membrane Fusion Mediated Targeted Cytosolic Drug Delivery Through scFv Engineered Sendai Viral Envelopes.
Kumar M, Mani P, Pratheesh P, Chandra S, Jeyakkodi M, Chattopadhyay P, Sarkar D, Sinha S. Membrane Fusion Mediated Targeted Cytosolic Drug Delivery Through scFv Engineered Sendai Viral Envelopes. 2015, 15: 386-400. PMID: 25941820, DOI: 10.2174/1566524015666150505155949.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAnimalsAntibiotics, AntineoplasticAntibodies, MonoclonalCell Line, TumorCHO CellsCricetinaeCricetulusCytoplasmDoxorubicinDrug Delivery SystemsFluorescein-5-isothiocyanateGPI-Linked ProteinsHeLa CellsHumansIsoenzymesMembrane FusionPeptide LibrarySendai virusStaining and LabelingViral Envelope ProteinsViral Fusion ProteinsConceptsOnco-fetal antigenF proteinNumber of malignanciesNative F proteinVariety of cancersAlkaline phosphataseViral envelopeCytoplasmic deliveryBreast cancerSendai viral envelopesSpecific antibodiesPAPPlacental isozymeCancerSpecific bindingAntibodiesDrugsDeliveryCytosolic drug deliveryPotential usefulnessRecombinant scFvReduced degradationHN proteinUbiquitous expression
2009
Fusion Loop Peptide of the West Nile Virus Envelope Protein Is Essential for Pathogenesis and Is Recognized by a Therapeutic Cross-Reactive Human Monoclonal Antibody
Sultana H, Foellmer HG, Neelakanta G, Oliphant T, Engle M, Ledizet M, Krishnan MN, Bonafé N, Anthony KG, Marasco WA, Kaplan P, Montgomery RR, Diamond MS, Koski RA, Fikrig E. Fusion Loop Peptide of the West Nile Virus Envelope Protein Is Essential for Pathogenesis and Is Recognized by a Therapeutic Cross-Reactive Human Monoclonal Antibody. The Journal Of Immunology 2009, 183: 650-660. PMID: 19535627, PMCID: PMC3690769, DOI: 10.4049/jimmunol.0900093.Peer-Reviewed Original ResearchConceptsWest Nile virus envelope proteinWest Nile virusVirus envelope proteinDengue virusCross-reactive human monoclonal antibodiesBlood-brain barrier permeabilityEnvelope proteinWest Nile virus infectionNeutralization escape variantsNile virusWest Nile encephalitisNeutralization escape mutantsHuman monoclonal antibodyFatal neurological diseaseParental West Nile virusFusion loopEscape variantsInflammatory responseBarrier permeabilityLethal encephalitisMAb11Virus infectionHuman mAbsEscape mutantsNeurological diseases
2008
Newcastle disease virus in West Africa: new virulent strains identified in non-commercial farms
Snoeck C, Ducatez M, Owoade A, Faleke O, Alkali B, Tahita M, Tarnagda Z, Ouedraogo J, Maikano I, Mbah P, Kremer J, Muller C. Newcastle disease virus in West Africa: new virulent strains identified in non-commercial farms. Archives Of Virology 2008, 154: 47-54. PMID: 19052688, DOI: 10.1007/s00705-008-0269-5.Peer-Reviewed Original Research
2006
Mutations of Conserved Glycine Residues within the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 gp41 Can Inhibit Membrane Fusion and Incorporation of Env onto Virions
Miyauchi K, Curran R, Matthews E, Komano J, Hoshino T, Engelman D, Matsuda Z. Mutations of Conserved Glycine Residues within the Membrane-Spanning Domain of Human Immunodeficiency Virus Type 1 gp41 Can Inhibit Membrane Fusion and Incorporation of Env onto Virions. Japanese Journal Of Infectious Diseases 2006, 59: 77-84. PMID: 16632906, DOI: 10.7883/yoken.jjid.2006.77.Peer-Reviewed Original Research
1999
Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion
Kahn J, Schnell M, Buonocore L, Rose J. Recombinant Vesicular Stomatitis Virus Expressing Respiratory Syncytial Virus (RSV) Glycoproteins: RSV Fusion Protein Can Mediate Infection and Cell Fusion. Virology 1999, 254: 81-91. PMID: 9927576, DOI: 10.1006/viro.1998.9535.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCricetinaeCytoplasmGene ExpressionGenetic VectorsGlycoproteinsHN ProteinHumansMembrane FusionMolecular Sequence DataRecombinant Fusion ProteinsRespiratory Syncytial Virus, HumanTumor Cells, CulturedVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsViral ProteinsVirionConceptsRecombinant vesicular stomatitis virusVesicular stomatitis virusRSV fusion proteinRSV F glycoproteinRSV vaccineF recombinantsRSV glycoproteinsRSV proteinsEnvelope glycoproteinVirus attachmentFusion (F) envelope glycoproteinsF glycoproteinG glycoproteinStomatitis virusLarge syncytiaGlycoproteinPH-independent pathwayCell surfaceCell fusionCytoplasmic tail sequencesVSV G.Endosomal pHFusion activityVaccineFusion protein
1996
Foreign 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 targeting
1995
Identification of a nef allele that causes lymphocyte activation and acute disease in Macaque monkeys
Du Z, Lang S, Sasseville V, Lackner A, Ilyinskii P, Daniel M, Jung J, Desrosiers R. Identification of a nef allele that causes lymphocyte activation and acute disease in Macaque monkeys. Cell 1995, 82: 665-674. PMID: 7664345, DOI: 10.1016/0092-8674(95)90038-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAllelesAmino Acid SequenceAnimalsBase SequenceDNA PrimersDNA, ViralGene Products, envGene Products, nefGenes, nefLymphocyte ActivationMacaca mulattaMiceMolecular Sequence DataPhagocytesPhenotypePhosphorylationRetroviridae Proteins, OncogenicSignal TransductionSimian Acquired Immunodeficiency SyndromeSimian immunodeficiency virusTransformation, GeneticTyrosineViral Fusion ProteinsVirus ReplicationConceptsAcute diseasePeripheral blood mononuclear cell culturesBlood mononuclear cell culturesMononuclear cell culturesT lymphocyte activationSevere diarrheaLymphoid proliferationsGastrointestinal tractNef allelesMacaque monkeysLymphocyte activationCellular activationSIVmac239NefDiseaseActivationMonkeysCell culturesImportant determinantCellsNIH 3T3 cellsTyrosine phosphorylationCotransfected COS cellsCOS cellsDiarrhea
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 serumCellsGlycoproteinExpressionReplicase
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 developmentCytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus
Owens R, Rose J. Cytoplasmic domain requirement for incorporation of a foreign envelope protein into vesicular stomatitis virus. Journal Of Virology 1993, 67: 360-365. PMID: 8093220, PMCID: PMC237371, DOI: 10.1128/jvi.67.1.360-365.1993.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCD4-Positive T-LymphocytesCell FusionFluorescent Antibody TechniqueGene Products, envHIV Envelope Protein gp120HIV Envelope Protein gp41HIV-1Membrane GlycoproteinsMolecular Sequence DataRecombinant Fusion ProteinsStructure-Activity RelationshipVesicular stomatitis Indiana virusViral Envelope ProteinsViral Fusion ProteinsConceptsHIV-1 envelope proteinEnvelope proteinAnti-HIV-1 seraHuman immunodeficiency virus type 1 (HIV-1) envelope proteinG proteinsHIV-1 entryVesicular stomatitis virus particlesHIV-1Vesicular stomatitis virusEnvelope glycoproteinWild-type G proteinStomatitis virusVSV particlesVSV G proteinVirus particlesTemperature-sensitive mutantPseudotypesSimultaneous expressionTransmembrane domainCytoplasmic domainCytoplasmic tailDefective transportVSV
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 crosslinkingStructural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein
Donnelly-Roberts D, Lentz T. Structural and conformational similarity between synthetic peptides of curaremimetic neurotoxins and rabies virus glycoprotein. Brain Research 1991, 11: 107-113. PMID: 1661807, DOI: 10.1016/0169-328x(91)90112-b.Peer-Reviewed Original ResearchConceptsLoop 2Virus glycoproteinAcetylcholine receptorsRabies virus glycoproteinBeta-sheet structureCircular dichroism spectroscopyCuraremimetic neurotoxinsAcetylcholine-binding siteSynthetic peptidesNicotinic acetylcholine receptorsDichroism spectroscopyStructural similarityConformational similarityCorresponding peptidesPolyclonal antibodiesGlycoproteinPeptides
1988
Cell-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 acids
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 linesTerminusGlycoproteinPeptidesMutagenesisOrganization of nonstructural genes of the autonomous parvovirus minute virus of mice
Cotmore S, Tattersall P. Organization of nonstructural genes of the autonomous parvovirus minute virus of mice. Journal Of Virology 1986, 58: 724-732. PMID: 2939261, PMCID: PMC252977, DOI: 10.1128/jvi.58.3.724-732.1986.Peer-Reviewed Original ResearchConceptsOpen reading frameAutonomous parvovirus minute virusParvovirus minute virusSimilar proteinsFusion proteinCommon amino-terminal sequenceSingle open reading frameNonstructural protein NS-1Rabbit reticulocyte lysate translation systemViral genomeReticulocyte lysate translation systemAlternative open reading framesNS-2 proteinsCarboxy-terminal halfNS-1 proteinNS-1Amino acid sequenceBacterial fusion proteinLysate translation systemMinute virusAmino-terminal sequenceProcaryotic expression vectorR2 transcriptsReading frameAcid sequence
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