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
1995
Minute virus of mice transcriptional activator protein NS1 binds directly to the transactivation region of the viral P38 promoter in a strictly ATP-dependent manner
Christensen J, Cotmore S, Tattersall P. Minute virus of mice transcriptional activator protein NS1 binds directly to the transactivation region of the viral P38 promoter in a strictly ATP-dependent manner. Journal Of Virology 1995, 69: 5422-5430. PMID: 7636987, PMCID: PMC189388, DOI: 10.1128/jvi.69.9.5422-5430.1995.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBase SequenceBinding SitesCell LineDeoxyribonuclease IDNA, ViralGenes, ViralGenetic VectorsGenome, ViralMinute virus of miceMolecular Sequence DataNucleopolyhedrovirusesPlasmidsPromoter Regions, GeneticRecombinant ProteinsSpodopteraTranscriptional ActivationTransfectionViral Nonstructural ProteinsViral ProteinsConceptsATP-dependent mannerGamma S-ATPTransactivation regionP38 promoterCognate sitesDNA fragmentsNS1 bindsCore DNA sequenceCarboxy-terminal peptidePotent transcriptional activatorMinute virusS-ATPTranscriptional activatorMVM genomeATP bindingTAR sequenceTATA boxDNA sequencesATP hydrolysisBiochemical stepsBp 5DNase INS1 polypeptideTAR bindingAntibodies
1989
Evidence for a ligation step in the DNA replication of the autonomous parvovirus minute virus of mice
Cotmore S, Gunther M, Tattersall P. Evidence for a ligation step in the DNA replication of the autonomous parvovirus minute virus of mice. Journal Of Virology 1989, 63: 1002-1006. PMID: 2911112, PMCID: PMC247784, DOI: 10.1128/jvi.63.2.1002-1006.1989.Peer-Reviewed Original Research
1988
The terminal protein of minute virus of mice is an 83 kilodalton polypeptide linked to specific forms of double‐stranded and single‐stranded viral DNA
Gunther M, Tattersall P. The terminal protein of minute virus of mice is an 83 kilodalton polypeptide linked to specific forms of double‐stranded and single‐stranded viral DNA. FEBS Letters 1988, 242: 22-26. PMID: 3203742, DOI: 10.1016/0014-5793(88)80977-3.Peer-Reviewed Original ResearchThe NS-1 polypeptide of minute virus of mice is covalently attached to the 5' termini of duplex replicative-form DNA and progeny single strands
Cotmore S, Tattersall P. The NS-1 polypeptide of minute virus of mice is covalently attached to the 5' termini of duplex replicative-form DNA and progeny single strands. Journal Of Virology 1988, 62: 851-860. PMID: 3339715, PMCID: PMC253642, DOI: 10.1128/jvi.62.3.851-860.1988.Peer-Reviewed Original Research
1987
The Autonomously Replicating Parvoviruses of Vertebrates
Cotmore S, Tattersall P. The Autonomously Replicating Parvoviruses of Vertebrates. Advances In Virus Research 1987, 33: 91-174. PMID: 3296697, DOI: 10.1016/s0065-3527(08)60317-6.Peer-Reviewed Original ResearchConceptsHost cellsProductive replicationHost cell typesSpecific cell surface receptorsHost cell factorsCell surface receptorsDifferentiated stateAutonomous parvovirusesIntracellular interactionsCell typesCell cyclingSurface receptorsCellular levelHelper virusCell factorWhole animalParvovirus strainsReplicationViral particlesPathogenic processesVertebratesCellsVirusParvovirusParvovirus group
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 expressionPolypeptideProteinOrganization 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 sequenceNucleotide 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 genomePolypeptideSequenceThe NS-1 polypeptide of the autonomous parvovirus MVM is a nuclear phosphoprotein
Cotmore S, Tattersall P. The NS-1 polypeptide of the autonomous parvovirus MVM is a nuclear phosphoprotein. Virus Research 1986, 4: 243-250. PMID: 3739422, DOI: 10.1016/0168-1702(86)90003-1.Peer-Reviewed Original ResearchConceptsParvovirus MVMNS-1 proteinVitro translation productsMessenger RNA speciesNS-1 polypeptideSame primary sequencePeptide map analysisNon-structural proteinsRNA speciesNuclear phosphoproteinReplication complexTranslation productsKb transcriptPrimary sequenceVivo productNS-1SpeciesProteinPredominant formPhosphoproteinMVMTranscriptsPolypeptideNucleusMap analysisDNA sequence of the lymphotropic variant of minute virus of mice, MVM(i), and comparison with the DNA sequence of the fibrotropic prototype strain
Astell C, Gardiner E, Tattersall P. DNA sequence of the lymphotropic variant of minute virus of mice, MVM(i), and comparison with the DNA sequence of the fibrotropic prototype strain. Journal Of Virology 1986, 57: 656-669. PMID: 3502703, PMCID: PMC252781, DOI: 10.1128/jvi.57.2.656-669.1986.Peer-Reviewed Original Research
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
1979
Parvoviridae: Second Report
Bachmann P, Hoggan D, Kurstak E, Melnick J, Pereira H, Tattersall P, Vago C. Parvoviridae: Second Report. Intervirology 1979, 11: 248-254. PMID: 372134, DOI: 10.1159/000149041.Peer-Reviewed Original Research
1977
Sequence homology between the structural polypeptides of minute virus of mice
Tattersall P, Shatkin A, Ward D. Sequence homology between the structural polypeptides of minute virus of mice. Journal Of Molecular Biology 1977, 111: 375-394. PMID: 864702, DOI: 10.1016/s0022-2836(77)80060-0.Peer-Reviewed Original ResearchConceptsA polypeptideEmpty virionsPolypeptide BTotal virion proteinsMinute virusPolypeptide speciesB polypeptidesSequence homologyPrecursor-product relationshipVirion proteinsC polypeptideStructural polypeptidesPolypeptideCommon sequenceEmpty particlesVirionsProteinDifferent conformationsEnzymePrevious kinetic studiesSequenceVivo observationsCleavageConformationVivo
1976
Three structural polypeptides coded for by minite virus of mice, a parvovirus
Tattersall P, Cawte P, Shatkin A, Ward D. Three structural polypeptides coded for by minite virus of mice, a parvovirus. Journal Of Virology 1976, 20: 273-289. PMID: 988192, PMCID: PMC354988, DOI: 10.1128/jvi.20.1.273-289.1976.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsAnimalsCell LineCricetinaeMinute virus of miceMolecular WeightParvoviridaePeptidesProteinsRatsViral ProteinsConceptsLate maturation stepPulse-chase experimentsNuclei of cellsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisDNA genomeSulfate-polyacrylamide gel electrophoresisThird polypeptideMaturation stepsVirion massProtein componentsHost cellsEmpty virionsStructural polypeptidesPolypeptideMinute virusGel electrophoresisCsCl gradientsProtein massUninfected cellsGrowth conditionsSequential harvestingEmpty particlesVirionsProtein