2014
Complementation for an essential ancillary non-structural protein function across parvovirus genera
Mihaylov IS, Cotmore SF, Tattersall P. Complementation for an essential ancillary non-structural protein function across parvovirus genera. Virology 2014, 468: 226-237. PMID: 25194919, PMCID: PMC4254310, DOI: 10.1016/j.virol.2014.07.043.Peer-Reviewed Original ResearchConceptsCell cycle progressionAncillary proteinsProtein functionDNA replicationReplication centersNP1 proteinPrimary sequenceFunctional overlapProtein NS2Cycle progressionGenus BocaparvovirusGenus ProtoparvovirusLate defectsNP1 inductionParvovirus genusVirion productionMinute virusSpecific defectsCell populationsUninfected cellsGenusCell viabilityProteinHuman bocavirus 1NP1 expression
2010
Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM)
Ruiz Z, Mihaylov IS, Cotmore SF, Tattersall P. Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM). Virology 2010, 410: 375-384. PMID: 21193212, PMCID: PMC3072075, DOI: 10.1016/j.virol.2010.12.009.Peer-Reviewed Original ResearchConceptsViral replication centersDamage responseReplication centersDamage response proteinsMutant infectionDNA damage responsePhosphorylation of ATRNS2 mutantsProtein recruitmentViral DNA amplificationATM activationCellular proteinsDNA replicationReplication factorsResponse proteinsBody maturationA9 cellsMVM infectionMinute virusWidespread associationWestern transferDNA amplificationMechanism of actionProteinRecruitment
1993
Nuclear Targeting of the Parvoviral Replicator Molecule NS1: Evidence for Self-Association Prior to Nuclear Transport
Nüesch J, Tattersall P. Nuclear Targeting of the Parvoviral Replicator Molecule NS1: Evidence for Self-Association Prior to Nuclear Transport. Virology 1993, 196: 637-651. PMID: 8372437, DOI: 10.1006/viro.1993.1520.Peer-Reviewed Original ResearchConceptsNuclear localizationMutant NS1 proteinsNS1 polypeptideMutant NS1Nuclear localization signalNS1 proteinMajor non-structural proteinsAmino acid substitutionsParvovirus minute virusNon-structural proteinsLocalization signalPutative NTPNuclear transportLysine motifNuclear targetingMammalian cellsSubstitution mutantsExpression systemAcid substitutionsFrame deletionDouble lysineProteinMinute virusSubcellular fractionsViral DNA
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
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 Research
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 expressionPolypeptideProteinThe 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 analysis
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
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 ResearchConceptsLate 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