2013
Parvoviral Left-End Hairpin Ears Are Essential during Infection for Establishing a Functional Intranuclear Transcription Template and for Efficient Progeny Genome Encapsidation
Li L, Cotmore SF, Tattersall P. Parvoviral Left-End Hairpin Ears Are Essential during Infection for Establishing a Functional Intranuclear Transcription Template and for Efficient Progeny Genome Encapsidation. Journal Of Virology 2013, 87: 10501-10514. PMID: 23903839, PMCID: PMC3807388, DOI: 10.1128/jvi.01393-13.Peer-Reviewed Original ResearchConceptsDNA replicationA9 cellsC-terminal transactivation domainCapsid gene expressionProtein expressionWild-type virionsProgeny virion productionP38 promoterTransactivation domainTranscription complexInfectious plasmid cloneGenome encapsidationGenome packagingAbsence of progenyGene expressionPlasmid clonesTranscription templateMutant virionsNonstructural proteinsReplacement vectorViral transcriptionViral transcriptsSuch complementationVirion stabilityDuplex DNA
1990
Alternate splicing in a parvoviral nonstructural gene links a common amino-terminal sequence to downstream domains which confer radically different localization and turnover characteristics
Cotmore S, Tattersall P. Alternate splicing in a parvoviral nonstructural gene links a common amino-terminal sequence to downstream domains which confer radically different localization and turnover characteristics. Virology 1990, 177: 477-487. PMID: 2142555, DOI: 10.1016/0042-6822(90)90512-p.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAphidicolinBase SequenceCapsidCell DivisionChromosome MappingDiterpenesFluorescent Antibody TechniqueGenes, ViralL CellsMiceMinute virus of miceMolecular Sequence DataMolecular WeightParvoviridaeRNA SplicingRNA, ViralSequence Homology, Nucleic AcidViral Core ProteinsViral Nonstructural ProteinsViral Structural ProteinsConceptsCommon amino-terminal domainAmino-terminal domainNS-1 moleculesCommon amino-terminal sequenceNS-1 polypeptideAmino-terminal sequenceSodium dodecyl sulfate gel electrophoresisNS-1Dodecyl sulfate gel electrophoresisUnphosphorylated formInternal exonsAlternate splicingGene productsSulfate gel electrophoresisA9 cellsNonstructural genesSpliced formsPhosphorylated formDownstream domainContiguous sequencesNonstructural proteinsSpecies migratePeptide-specific antibodiesMinute virusTurnover characteristicsSusceptibility of human cells to killing by the parvoviruses H-1 and minute virus of mice correlates with viral transcription
Cornelis J, Chen Y, Spruyt N, Duponchel N, Cotmore S, Tattersall P, Rommelaere J. Susceptibility of human cells to killing by the parvoviruses H-1 and minute virus of mice correlates with viral transcription. Journal Of Virology 1990, 64: 2537-2544. PMID: 2139892, PMCID: PMC249429, DOI: 10.1128/jvi.64.6.2537-2544.1990.Peer-Reviewed Original ResearchConceptsViral mRNAsHuman cellsLevel of transcriptionMinute virusMajor viral transcriptViral DNA amplificationNonstructural polypeptidesGene productsOncogenic transformationGene expressionIntracellular localizationNonstructural proteinsViral transcriptionViral transcriptsTranscriptionViral genomeParvovirus HCell susceptibilityHuman fibroblastsVirus uptakeEpithelial cellsDNA amplificationResistant derivativesKeratinocyte lineDifferential susceptibility
1989
Limitations to the expression of parvoviral nonstructural proteins may determine the extent of sensitization of EJ-ras-transformed rat cells to minute virus of mice
Van Hille B, Duponchel N, Salomé N, Spruyt N, Cotmore S, Tattersall P, Cornelis J, Rommelaere J. Limitations to the expression of parvoviral nonstructural proteins may determine the extent of sensitization of EJ-ras-transformed rat cells to minute virus of mice. Virology 1989, 171: 89-97. PMID: 2525841, DOI: 10.1016/0042-6822(89)90514-x.Peer-Reviewed Original ResearchConceptsNonstructural proteinsNonstructural protein NS-1Parvoviral DNA replicationRat cellsParvoviral life cycleNonstructural viral proteinsDNA replicationRat cell linesSensitivity of cellsRas transformationP21ras proteinsNormal rat cellsGene expressionMVMp infectionParvovirus MVMpNRK cellsViral proteinsEarly blockProteinCell linesViral DNALife cycleNS-1MVMpExpression
1986
Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments
Cotmore S, McKie V, Anderson L, Astell C, Tattersall P. Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments. Journal Of Virology 1986, 60: 548-557. PMID: 3021988, PMCID: PMC288924, DOI: 10.1128/jvi.60.2.548-557.1986.Peer-Reviewed Original ResearchConceptsProtein sequencesViral capsid polypeptidesCapsid polypeptidesSucrose velocity gradientsB19 genomeBacterial plasmid vectorRestriction endonuclease fragmentsGenomic fragmentProtein speciesApparent molecular weightNonstructural polypeptidesExpression constructsSimilar proteinsBAL-31GenomeExpression vectorNonstructural proteinsEndonuclease fragmentsPlasmid vectorViral genomeViral polypeptidesPolypeptide fragmentsProcaryotic expressionPolypeptideProteinNucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis
Shade R, Blundell M, Cotmore S, Tattersall P, Astell C. Nucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis. Journal Of Virology 1986, 58: 921-936. PMID: 3701931, PMCID: PMC253001, DOI: 10.1128/jvi.58.3.921-936.1986.Peer-Reviewed Original ResearchConceptsNucleotide sequenceLarge open reading frameMajor nonstructural proteinOpen reading frameFull-length cloneMajor structural polypeptidesGenome organizationGenomic clonesPutative polypeptideTranscription unitEntire genomeReading frameDNA sequencesFourth promoterParvovirus genomeSequence informationNonstructural proteinsGenomeTerminal repeatDependovirus genusStructural polypeptidesViral DNAB19 genomePolypeptideSequence
1983
The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides
Cotmore S, Sturzenbecker L, Tattersall P. The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides. Virology 1983, 129: 333-343. PMID: 6623929, DOI: 10.1016/0042-6822(83)90172-1.Peer-Reviewed Original ResearchConceptsParvovirus MVMCapsid polypeptidesNS-1 proteinOpen reading frameNS-1 polypeptidePeptide map analysisMajor intronTranscription unitMVM genomeVitro translationApparent molecular weightReading frameNonstructural proteinsPolypeptideProteinVP-1NS-1VP-2GenomeIntronsComigratesMolecular weightTranscriptsMVMMap analysis