2001
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
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
1999
Two New Members of the Emerging KDWK Family of Combinatorial Transcription Modulators Bind as a Heterodimer to Flexibly Spaced PuCGPy Half-Sites
Christensen J, Cotmore S, Tattersall P. Two New Members of the Emerging KDWK Family of Combinatorial Transcription Modulators Bind as a Heterodimer to Flexibly Spaced PuCGPy Half-Sites. Molecular And Cellular Biology 1999, 19: 7741-7750. PMID: 10523663, PMCID: PMC84824, DOI: 10.1128/mcb.19.11.7741.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBinding SitesCloning, MolecularDimerizationDNA-Binding ProteinsDNA, ComplementaryGC Rich SequenceHeLa CellsHumansMolecular Sequence DataMultigene FamilyNuclear ProteinsParvovirusPromoter Regions, GeneticProtein BindingReceptors, TransferrinRecombinant ProteinsReplication OriginSequence Homology, Amino AcidTranscription FactorsTyrosine TransaminaseConceptsParvovirus initiation factorPromoter activation assaysParvovirus DNA replicationE-box motifAmino acid identityTransferrin receptor promoterResponse element-binding proteinCyclic AMP response element binding proteinElement-binding proteinHeLa factorsAMP response element binding proteinTranscriptional modulatorDNA replicationHuman cDNAAcid identityInitiation factorsRegulatory elementsDEAF-1Recombinant baculovirusHalf sitesPromoter regionComplex bindsReceptor promoterHost cellsComplex consistingControlled Conformational Transitions in the MVM Virion Expose the VP1 N-Terminus and Viral Genome without Particle Disassembly
Cotmore S, D'Abramo A, Ticknor C, Tattersall P. Controlled Conformational Transitions in the MVM Virion Expose the VP1 N-Terminus and Viral Genome without Particle Disassembly. Virology 1999, 254: 169-181. PMID: 9927584, DOI: 10.1006/viro.1998.9520.Peer-Reviewed Original ResearchConceptsViral particlesPrior treatmentAntigenic determinantsCapsid protein VP1Empty viral particlesParvovirus minute virusBrief exposureInfectious virionsIndividual polypeptide speciesSerumProtein VP1Proportion of virionsVirusVirionsEpitope accessibilityMinute virusApparent integrityViral genomeGreat majorityVP1ProportionMice
1998
Functional implications of the structure of the murine parvovirus, minute virus of mice
Agbandje-McKenna M, Llamas-Saiz A, Wang F, Tattersall P, Rossmann M. Functional implications of the structure of the murine parvovirus, minute virus of mice. Structure 1998, 6: 1369-1381. PMID: 9817841, DOI: 10.1016/s0969-2126(98)00137-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCapsidCapsid ProteinsGlycineMinute virus of miceMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidTropismConceptsAmino acidsUnique N-terminal regionThree-dimensional structure determinationC-terminal regionDNA recognition siteN-terminal regionGlycine-rich sequenceMinute virusTissue tropismHost cell factorsCanine parvovirusDNA packagingIcosahedral asymmetric unitN-terminal peptideN-terminusMurine parvovirusTissue specificityStructural proteinsPolypeptide chainFivefold channelCapsid proteinViral genomeFunctional implicationsRecognition sitesVirus structure
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 ResearchConceptsDNA-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-Binding ProteinsDNA, RecombinantGenome, 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 virusVTF7-3Two amino acid substitutions within the capsid are coordinately required for acquisition of fibrotropism by the lymphotropic strain of minute virus of mice
Ball-Goodrich L, Tattersall P. Two amino acid substitutions within the capsid are coordinately required for acquisition of fibrotropism by the lymphotropic strain of minute virus of mice. Journal Of Virology 1992, 66: 3415-3423. PMID: 1316457, PMCID: PMC241122, DOI: 10.1128/jvi.66.6.3415-3423.1992.Peer-Reviewed Original ResearchConceptsRestrictive infectionDouble mutant virusLymphotropic strainViral life cycleMinute virusInfectionImmunosuppressive strainFibroblast infectionVirusParvovirus minute virusMutant virusA9 fibroblastsCodon 317MiceCodon 321Amino acid substitutionsFibroblastsSame cellsCapsid geneCellsGene expressionAcid substitutionsSynergistic interactionNucleotide changesA9 cells
1991
Parvoviral target cell specificity: Acquisition of fibrotropism by a mutant of the lymphotropic strain of minute virus of mice involves multiple amino acid substitutions within the capsid
Ball-Goodrich L, Moir R, Tattersall P. Parvoviral target cell specificity: Acquisition of fibrotropism by a mutant of the lymphotropic strain of minute virus of mice involves multiple amino acid substitutions within the capsid. Virology 1991, 184: 175-186. PMID: 1871965, DOI: 10.1016/0042-6822(91)90834-x.Peer-Reviewed Original ResearchConceptsCoat protein geneProtein geneA9 fibroblastsInfectious cloneAmino acidsSite-directed mutagenesisMinute virusMultiple amino acid substitutionsSingle base changeAmino acid substitutionsGlutamic acid residuesSame amino acidsMouse A9 fibroblastsDouble mutantSame small regionA9 cellsHost rangeAcid residuesMutantsAcid substitutionsT lymphocyte cell lineDNA sequencingRecombinants
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 characteristics
1988
Mapping of the fibrotropic and lymphotropic host range determinants of the parvovirus minute virus of mice
Gardiner E, Tattersall P. Mapping of the fibrotropic and lymphotropic host range determinants of the parvovirus minute virus of mice. Journal Of Virology 1988, 62: 2605-2613. PMID: 3392768, PMCID: PMC253690, DOI: 10.1128/jvi.62.8.2605-2613.1988.Peer-Reviewed Original ResearchConceptsFibroblast host cellsLymphotropic strainHost cell typesLymphocyte culturesMinute virusPlaque formationTarget cell specificityChimeric viral genomesFibroblast monolayersViral growthParvovirus minute virusViral progenyVirusHost range determinantsMiceHost cellsCell specificityCell typesRecombinant virusesViral sequencesViral genomeViral promotersInfectious genomic cloneVirus structural genesRange determinants