2017
The MVMp P4 promoter is a host cell-type range determinant in vivo
Meir C, Mincberg M, Rostovsky I, Tal S, Vollmers EM, Levi A, Tattersall P, Davis C. The MVMp P4 promoter is a host cell-type range determinant in vivo. Virology 2017, 506: 141-151. PMID: 28391161, DOI: 10.1016/j.virol.2017.03.012.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsGene Expression Regulation, ViralHost SpecificityMiceMinute virus of miceParvoviridae InfectionsPromoter Regions, GeneticRodent DiseasesViral Nonstructural ProteinsVirus Replication
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 ResearchMeSH KeywordsAnimalsCell LineDNA RepairDNA ReplicationDNA, ViralHost-Pathogen InteractionsMiceMinute virus of miceProteinsViral Nonstructural ProteinsVirus ReplicationConceptsViral 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
2001
The Left-End and Right-End Origins of Minute Virus of Mice DNA Differ in Their Capacity to Direct Episomal Amplification and Integration In Vivo
Corsini J, Cotmore S, Tattersall P, Winocour E. The Left-End and Right-End Origins of Minute Virus of Mice DNA Differ in Their Capacity to Direct Episomal Amplification and Integration In Vivo. Virology 2001, 288: 154-163. PMID: 11543668, DOI: 10.1006/viro.2001.1076.Peer-Reviewed Original ResearchMeSH Keywords5' Untranslated RegionsAnimalsCell LineDNA ReplicationDNA, ViralHeLa CellsHumansMiceMinute virus of micePlasmidsViral Nonstructural ProteinsVirus IntegrationVirus ReplicationMinute Virus of Mice Initiator Protein NS1 and a Host KDWK Family Transcription Factor Must Form a Precise Ternary Complex with Origin DNA for Nicking To Occur
Christensen J, Cotmore S, Tattersall P. Minute Virus of Mice Initiator Protein NS1 and a Host KDWK Family Transcription Factor Must Form a Precise Ternary Complex with Origin DNA for Nicking To Occur. Journal Of Virology 2001, 75: 7009-7017. PMID: 11435581, PMCID: PMC114429, DOI: 10.1128/jvi.75.15.7009-7017.2001.Peer-Reviewed Original Research
2000
Two Widely Spaced Initiator Binding Sites Create an HMG1-Dependent Parvovirus Rolling-Hairpin Replication Origin
Cotmore S, Christensen J, Tattersall P. Two Widely Spaced Initiator Binding Sites Create an HMG1-Dependent Parvovirus Rolling-Hairpin Replication Origin. Journal Of Virology 2000, 74: 1332-1341. PMID: 10627544, PMCID: PMC111468, DOI: 10.1128/jvi.74.3.1332-1341.2000.Peer-Reviewed Original Research
1998
High-Mobility Group 1/2 Proteins Are Essential for Initiating Rolling-Circle-Type DNA Replication at a Parvovirus Hairpin Origin
Cotmore S, Tattersall P. High-Mobility Group 1/2 Proteins Are Essential for Initiating Rolling-Circle-Type DNA Replication at a Parvovirus Hairpin Origin. Journal Of Virology 1998, 72: 8477-8484. PMID: 9765384, PMCID: PMC110256, DOI: 10.1128/jvi.72.11.8477-8484.1998.Peer-Reviewed Original ResearchBiochemical Activities of Minute Virus of Mice Nonstructural Protein NS1 Are Modulated In Vitro by the Phosphorylation State of the Polypeptide
Nüesch J, Corbau R, Tattersall P, Rommelaere J. Biochemical Activities of Minute Virus of Mice Nonstructural Protein NS1 Are Modulated In Vitro by the Phosphorylation State of the Polypeptide. Journal Of Virology 1998, 72: 8002-8012. PMID: 9733839, PMCID: PMC110136, DOI: 10.1128/jvi.72.10.8002-8012.1998.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceDNA HelicasesDNA PrimersEnzyme ActivationHeLa CellsHumansMinute virus of micePhosphorylationViral Nonstructural ProteinsConceptsHelicase activityBiochemical activityMultifunctional nuclear phosphoproteinEndogenous protein kinaseMajor nonstructural proteinIntrinsic helicase activityViral DNA replicationMinute virusCalf intestine alkaline phosphataseTarget DNA sequenceReplication extractThreonine residuesNonstructural protein NS1Particular phosphorylationInitiator proteinDNA replicationIntrinsic ATPasePosttranslational modificationsDNA motifsCellular promotersNuclear phosphoproteinProtein kinaseNickase activityDNA sequencesPhosphorylation state
1997
Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs
Christensen J, Cotmore S, Tattersall P. Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs. Journal Of Virology 1997, 71: 5733-5741. PMID: 9223459, PMCID: PMC191825, DOI: 10.1128/jvi.71.8.5733-5741.1997.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBinding SitesDNADNA-Binding ProteinsHeLa CellsHumansMinute virus of miceMolecular Sequence DataMolecular WeightOligonucleotidesSpodopteraViral Nonstructural ProteinsConceptsDNA-binding factorsACGT motifGel mobility shift assaysReplication initiation processMobility shift assaysHigher-order multimersParvovirus initiation factorSame cellular factorHeLa S3 cellsMouse genomeBinds DNADNA replicationACGT sequenceInitiation factorsOrigin sequencesShift assaysMinimal originMutant oligonucleotidesATP hydrolysisMobility shiftDNase ICellular factorsEssential cofactorMobility assaysSingle binding siteThe NS2 Polypeptide of Parvovirus MVM Is Required for Capsid Assembly in Murine Cells
Cotmore S, D'abramo A, Carbonell L, Bratton J, Tattersall P. The NS2 Polypeptide of Parvovirus MVM Is Required for Capsid Assembly in Murine Cells. Virology 1997, 231: 267-280. PMID: 9168889, DOI: 10.1006/viro.1997.8545.Peer-Reviewed Original ResearchA novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication
Christensen J, Cotmore S, Tattersall P. A novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication. Journal Of Virology 1997, 71: 1405-1416. PMID: 8995666, PMCID: PMC191197, DOI: 10.1128/jvi.71.2.1405-1416.1997.Peer-Reviewed Original ResearchConceptsReplication protein AProliferating-cell nuclear antigenOrigin replicationDNA replicationSite-specific DNA-binding proteinRecombinant replication protein AUV cross-linking analysisParvovirus DNA replicationDNA-binding proteinsSequence-specific DNACross-linking analysisSimian virus 40 replicationParvovirus initiation factorCellular proteinsInitiation factorsTranscription factorsEndonuclease functionMinimal originGel shiftMVM replicationNS1 polypeptideSpecific nickingS100 extractsSite regionDNA proceeds
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 bindingAntibodiesSequence Motifs in the Replicator Protein of Parvovirus MVM Essential for Nicking and Covalent Attachment to the Viral Origin: Identification of the Linking Tyrosine
Nüesch J, Cotmore S, Tattersall P. Sequence Motifs in the Replicator Protein of Parvovirus MVM Essential for Nicking and Covalent Attachment to the Viral Origin: Identification of the Linking Tyrosine. Virology 1995, 209: 122-135. PMID: 7747462, DOI: 10.1006/viro.1995.1236.Peer-Reviewed Original ResearchConceptsMutant proteinsRolling-circle replicationTyrosine motifOrigin-containing plasmidParvoviral DNA replicationViral originParvovirus minute virusSingle-strand nicksInitiator proteinSequence motifsDNA replicationSite-specific bindingSequence comparisonCyanogen bromide cleavageOrigin sequencesDe novo synthesisSubstrate DNAY210Circle replicationLatter residueStrand nicksHeLa cellsLow salt conditionsCommon motifMetal coordination sitesThe NS1 polypeptide of the murine parvovirus minute virus of mice binds to DNA sequences containing the motif [ACCA]2-3
Cotmore S, Christensen J, Nüesch J, Tattersall P. The NS1 polypeptide of the murine parvovirus minute virus of mice binds to DNA sequences containing the motif [ACCA]2-3. Journal Of Virology 1995, 69: 1652-1660. PMID: 7853501, PMCID: PMC188764, DOI: 10.1128/jvi.69.3.1652-1660.1995.Peer-Reviewed Original Research
1994
An asymmetric nucleotide in the parvoviral 3′ hairpin directs segregation of a single active origin of DNA replication.
Cotmore S, Tattersall P. An asymmetric nucleotide in the parvoviral 3′ hairpin directs segregation of a single active origin of DNA replication. The EMBO Journal 1994, 13: 4145-4152. PMID: 8076610, PMCID: PMC395337, DOI: 10.1002/j.1460-2075.1994.tb06732.x.Peer-Reviewed Original Research
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 DNAAsymmetric resolution of a parvovirus palindrome in vitro
Cotmore S, Nüesch J, Tattersall P. Asymmetric resolution of a parvovirus palindrome in vitro. Journal Of Virology 1993, 67: 1579-1589. PMID: 8437230, PMCID: PMC237529, DOI: 10.1128/jvi.67.3.1579-1589.1993.Peer-Reviewed Original ResearchAnimalsBase SequenceCloning, MolecularDeoxyribonucleases, Type II Site-SpecificDNA ReplicationDNA, RecombinantDNA-Binding ProteinsGenome, ViralHeLa CellsHumansL CellsMiceMinute virus of miceMolecular Sequence DataNucleic Acid ConformationSubstrate SpecificityTelomereViral Nonstructural ProteinsVirus Replication
1992
Expression of functional parvoviral NS1 from recombinant vaccinia virus: Effects of mutations in the nucleotide-binding motif
Noesch J, Cotmore S, Tattersall P. Expression of functional parvoviral NS1 from recombinant vaccinia virus: Effects of mutations in the nucleotide-binding motif. Virology 1992, 191: 406-416. PMID: 1413512, DOI: 10.1016/0042-6822(92)90202-z.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological TransportBlotting, WesternCell LineCell NucleusCloning, MolecularDNA ReplicationDNA, ViralGenes, ViralHumansMiceMinute virus of miceMolecular Sequence DataPlasmidsPolymerase Chain ReactionRecombinant ProteinsTranscriptional ActivationVaccinia virusViral Nonstructural ProteinsConceptsWild-type NS1Mutant formsEfficient cap-independent translationVaccinia thymidine kinase geneNucleotide-binding motifCap-independent translationBacteriophage T7 promoterT7 RNA polymeraseEffects of mutationsThymidine kinase geneExpression of NS1Recombinant vaccinia virusP38 promoterRNA polymeraseReplicative proteinsChromosomal sitesLysine codonPurine triphosphatesKinase geneT7 promoterUntranslated regionMouse cellsNuclear extractsVaccinia virusVTF7-3In vitro excision and replication of 5′ telomeres of minute virus of mice DNA from cloned palindromic concatemer junctions
Cotmore S, Nuesch J, Tattersall P. In vitro excision and replication of 5′ telomeres of minute virus of mice DNA from cloned palindromic concatemer junctions. Virology 1992, 190: 365-377. PMID: 1388310, DOI: 10.1016/0042-6822(92)91223-h.Peer-Reviewed Original ResearchThe pathogenesis of infection with minute virus of mice depends on expression of the small nonstructural protein NS2 and on the genotype of the allotropic determinants VP1 and VP2
Brownstein D, Smith A, Johnson E, Pintel D, Naeger L, Tattersall P. The pathogenesis of infection with minute virus of mice depends on expression of the small nonstructural protein NS2 and on the genotype of the allotropic determinants VP1 and VP2. Journal Of Virology 1992, 66: 3118-3124. PMID: 1373202, PMCID: PMC241074, DOI: 10.1128/jvi.66.5.3118-3124.1992.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnimals, NewbornCapsidDNA, ViralEpitopesGenetic VariationImmunohistochemistryMiceMice, Inbred C3HMinute virus of miceMutagenesisNucleic Acid HybridizationParvoviridae InfectionsStructure-Activity RelationshipTissue DistributionViral Core ProteinsViral Nonstructural ProteinsVirulenceConceptsPathogenesis of infectionAsymptomatic infectionMultiple organsViral capsid antigenMesenteric lymph nodesSmooth muscle cellsSame target cellsMVMi infectionLymph nodesCapsid antigenMVMp infectionLethal infectionC3H/Lymphoid cellsTarget organsSimilar dosesAllotropic determinantMinute virusInfectious virusVirus titrationInfectionMuscle cellsMiceTitersTarget cells