2001
An Effective AIDS Vaccine Based on Live Attenuated Vesicular Stomatitis Virus Recombinants
Rose N, Marx P, Luckay A, Nixon D, Moretto W, Donahoe S, Montefiori D, Roberts A, Buonocore L, Rose J. An Effective AIDS Vaccine Based on Live Attenuated Vesicular Stomatitis Virus Recombinants. Cell 2001, 106: 539-549. PMID: 11551502, DOI: 10.1016/s0092-8674(01)00482-2.Peer-Reviewed Original ResearchMeSH KeywordsAcquired Immunodeficiency SyndromeAIDS VaccinesAnimalsCD4 Lymphocyte CountCD4-Positive T-LymphocytesEnzyme-Linked Immunosorbent AssayGene Products, envGene Products, gagHIVHIV AntibodiesHumansImmunization, SecondaryMacaca mulattaMiceNeutralization TestsPilot ProjectsRecombinant Fusion ProteinsSAIDS VaccinesSimian Acquired Immunodeficiency SyndromeSimian immunodeficiency virusTime FactorsT-Lymphocytes, CytotoxicVaccines, AttenuatedVaccines, SyntheticVesicular stomatitis Indiana virusViral LoadVirus Shedding
2000
Successful Vaccine-Induced Seroconversion by Single-Dose Immunization in the Presence of Measles Virus-Specific Maternal Antibodies
Schlereth B, Rose J, Buonocore L, Meulen V, Niewiesk S. Successful Vaccine-Induced Seroconversion by Single-Dose Immunization in the Presence of Measles Virus-Specific Maternal Antibodies. Journal Of Virology 2000, 74: 4652-4657. PMID: 10775601, PMCID: PMC111985, DOI: 10.1128/jvi.74.10.4652-4657.2000.Peer-Reviewed Original ResearchConceptsMV-specific antibodiesMaternal antibodiesVesicular stomatitis virusMV hemagglutininVaccine-induced seroconversionCotton rat modelRecombinant vesicular stomatitis virusSingle-dose immunizationInduction of antibodiesSuccessful immunizationVirus doseRat modelSuccessful vaccineRat antibodiesSubsequent challengeMeasles virusDissociation of functionHigh titersImmunizationAntibodiesSeroconversionStomatitis virusInductionVirusHemagglutininExpression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope
Haglund K, Forman J, Kräusslich H, Rose J. Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope. Virology 2000, 268: 112-121. PMID: 10683333, DOI: 10.1006/viro.1999.0120.Peer-Reviewed Original ResearchMeSH KeywordsAIDS VaccinesAnimalsCell LineDNA, RecombinantGene Products, gagGenetic VectorsHIV Envelope Protein gp120HIV-1HumansMembrane GlycoproteinsMicroscopy, ElectronPlasmidsProtein PrecursorsRecombinant Fusion ProteinsVaccines, AttenuatedVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsHIV virus-like particlesVirus-like particlesEnv proteinHIV-1HIV-1 envelope proteinAntibody-mediated immunityHigh-level productionRecombinant vesicular stomatitis virusVSV particlesHIV Env proteinEnvelope proteinEffective vaccine vectorHIV-like particlesProtein precursorHIV envelopeHigh-level expression vectorVaccine vectorHIV recombinantsVesicular stomatitis virusVirus titersVirus recombinantsVSV G proteinG proteinsStomatitis virusExpression vector
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 recombinantsRecombinant 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 proteinRedesign and Genetic Dissection of The Rhabdoviruses
Roberts A, Rose J. Redesign and Genetic Dissection of The Rhabdoviruses. Advances In Virus Research 1999, 53: 301-319. PMID: 10582104, DOI: 10.1016/s0065-3527(08)60353-x.Peer-Reviewed Original ResearchConceptsNegative-strand RNA virusesGenetic dissectionNegative-strand genome RNAWild-type virusRNA virusesNonsegmented negative-strand RNA virusesBacteriophage T7 RNA polymeraseNegative-strand RNA genomeVaccine vector developmentT7 RNA polymeraseRNA polymeraseInfection of cellsT7 promoterGenome RNARNA genomeGenetic analysisPolymerase proteinNNS virusesViral transcriptionNotorious pathogenViral assemblyRhabdovirusDNA copiesRecombinant virusesPlasmid DNA
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 proteinTailHybridsRequirement 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 geneCD4CXCR4Specific targeting to CD4+ cells of recombinant vesicular stomatitis viruses encoding human immunodeficiency virus envelope proteins
Johnson J, Schnell M, Buonocore L, Rose J. Specific targeting to CD4+ cells of recombinant vesicular stomatitis viruses encoding human immunodeficiency virus envelope proteins. Journal Of Virology 1997, 71: 5060-5068. PMID: 9188571, PMCID: PMC191739, DOI: 10.1128/jvi.71.7.5060-5068.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCD4-Positive T-LymphocytesCell LineCricetinaeGene ExpressionGenetic VectorsHeLa CellsHIV Envelope Protein gp160HIV-1HumansMembrane GlycoproteinsProtein Processing, Post-TranslationalRabbitsRecombinant Fusion ProteinsRecombination, GeneticVesicular stomatitis Indiana virusViral Envelope ProteinsVirionConceptsRecombinant vesicular stomatitis virusHuman immunodeficiency virus envelope proteinHIV envelope proteinVesicular stomatitis virusHIV envelopeVirus envelope proteinEnvelope proteinHIV type 1 envelopeChimeric envelopesCD4-positive cellsReplication-competent recombinant virusesStomatitis virusHIV seraRecombinant virusesHIV vaccineSpecific infectionsPrimary isolatesHIV-1HIV gp120Chimeric envelope proteinsAlternative receptorLow titersVSV serumVSV infectivityVSV glycoprotein
1996
Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains.
Rodgers W, Rose J. Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains. Journal Of Cell Biology 1996, 135: 1515-1523. PMID: 8978819, PMCID: PMC2133949, DOI: 10.1083/jcb.135.6.1515.Peer-Reviewed Original ResearchConceptsExclusion of CD45Low kinase activityGEM fractionMembrane domainsKinase activitySrc family tyrosine kinasesReservoir of enzymesSpecific membrane domainsActivity of p56lckTyrosine phosphatase CD45Family tyrosine kinasesT cell developmentTX-100-soluble fractionGEM domainsPhosphatase CD45Membrane proteinsKinase specific activityLckTyrosine kinaseMembrane fractionJurkat cellsPeptide mappingP56lckPhosphorylationHyperphosphorylationReplication 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 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
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-DirectedMyristatesPalmitatesProteinsProtein-Tyrosine KinasesStructure-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 disruptionMutations 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
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 surfaceHIVBlockadeCell 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 development