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
2013
Distinct host cell fates for human malignant melanoma targeted by oncolytic rodent parvoviruses
Vollmers EM, Tattersall P. Distinct host cell fates for human malignant melanoma targeted by oncolytic rodent parvoviruses. Virology 2013, 446: 37-48. PMID: 24074565, PMCID: PMC3811133, DOI: 10.1016/j.virol.2013.07.013.Peer-Reviewed Original ResearchConceptsPrimary human melanoma cellsPatient-derived melanoma cell linesCurrent therapeutic regimensHuman malignant melanomaRodent parvovirusesHuman melanoma cellsLow response rateMelanoma cell linesOncolytic parvovirusTherapeutic regimensMetastatic melanomaMalignant melanomaResponse rateVirion uptakeViral protein synthesisHost cell fateChimeric virusesMelanoma cellsComplete lysisCell linesMelanomaViral transcriptionParvovirusProgeny virionsLow multiplicity
2011
The parvoviral capsid controls an intracellular phase of infection essential for efficient killing of stepwise-transformed human fibroblasts
Paglino J, Tattersall P. The parvoviral capsid controls an intracellular phase of infection essential for efficient killing of stepwise-transformed human fibroblasts. Virology 2011, 416: 32-41. PMID: 21600623, PMCID: PMC3112476, DOI: 10.1016/j.virol.2011.04.015.Peer-Reviewed Original Research
2001
A consensus DNA recognition motif for two KDWK transcription factors identifies flexible-length, CpG-methylation sensitive cognate binding sites in the majority of human promoters11Edited by M. Yaniv
Burnett E, Christensen J, Tattersall P. A consensus DNA recognition motif for two KDWK transcription factors identifies flexible-length, CpG-methylation sensitive cognate binding sites in the majority of human promoters11Edited by M. Yaniv. Journal Of Molecular Biology 2001, 314: 1029-1039. PMID: 11743720, DOI: 10.1006/jmbi.2000.5198.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsBase SequenceBinding SitesConsensus SequenceCpG IslandsDimerizationDNADNA MethylationDNA-Binding ProteinsElectrophoretic Mobility Shift AssayHeLa CellsHumansKineticsMolecular WeightPromoter Regions, GeneticProtein BindingProtein SubunitsResponse ElementsSubstrate SpecificityTranscription FactorsConceptsParvovirus initiation factorTranscription factorsDNA recognition motifDNA-binding heterodimersParvoviral DNA replicationTranscriptional start siteCellular transcription factorsEukaryotic genomesProtein complexesDNA replicationM. YanivInitiation factorsStart siteCpG methylationHuman promotersRecognition motifCytosine residuesRecombinant baculovirusSelection experimentsElement upstreamC residuesHeLa cellsPromoterHeterodimersHost factorsThe 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 ResearchMinute 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 ResearchAutonomous Parvoviruses as Gene Transfer Vehicles
Palmer G, Tattersall P. Autonomous Parvoviruses as Gene Transfer Vehicles. Contributions To Microbiology 2000, 4: 178-202. PMID: 10941578, DOI: 10.1159/000060337.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 consistingcis Requirements for the Efficient Production of Recombinant DNA Vectors Based on Autonomous Parvoviruses
Kestler J, Neeb B, Struyf S, Van Damme J, Cotmore S, D'Abramo A, Tattersall P, Rommelaere J, Dinsart C, Cornelis J. cis Requirements for the Efficient Production of Recombinant DNA Vectors Based on Autonomous Parvoviruses. Human Gene Therapy 1999, 10: 1619-1632. PMID: 10428207, DOI: 10.1089/10430349950017626.Peer-Reviewed Original ResearchConceptsViral vectorsViral vector productionRecombinant viral vectorsRecombinant DNA vectorsVector productionRecombinant parvovirusesDNA vectorsRecombinant particlesVirus vectorsOverall sizeRecombinant vectorSmall transgenesEfficient productionHelper plasmidForeign DNAEfficient packagingPlasmid DNAParvovirus MVMpRecombinant clonesAutonomous parvovirusesViral terminiInfectious unitsVP sequencesDNA lengthVector
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 ResearchConceptsHelicase 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 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
Sequence 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 sites
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 virusVTF7-3In 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 Research