2017
Cryo-EM maps reveal five-fold channel structures and their modification by gatekeeper mutations in the parvovirus minute virus of mice (MVM) capsid
Subramanian S, Organtini LJ, Grossman A, Domeier PP, Cifuente JO, Makhov AM, Conway JF, D'Abramo A, Cotmore SF, Tattersall P, Hafenstein S. Cryo-EM maps reveal five-fold channel structures and their modification by gatekeeper mutations in the parvovirus minute virus of mice (MVM) capsid. Virology 2017, 510: 216-223. PMID: 28750325, PMCID: PMC5601314, DOI: 10.1016/j.virol.2017.07.015.Peer-Reviewed Original ResearchThe 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 Research
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 DNAParvovirus evades interferon-dependent viral control in primary mouse embryonic fibroblasts
Mattei LM, Cotmore SF, Tattersall P, Iwasaki A. Parvovirus evades interferon-dependent viral control in primary mouse embryonic fibroblasts. Virology 2013, 442: 20-27. PMID: 23676303, PMCID: PMC3767977, DOI: 10.1016/j.virol.2013.03.020.Peer-Reviewed Original ResearchConceptsType I IFNsI IFNsI interferonIFN responseAntiviral immune mechanismsType I interferonInnate defense mechanismsMouse embryonic fibroblastsMVMp infectionViral controlImmune mechanismsInnate sensingAntiviral programViral replicationViral sensorsMurine parvovirusPoly (I:C) stimulationVirusEmbryonic fibroblastsType IMiceDefense mechanismsMinute virusMVMpPrimary mouse embryonic fibroblasts
2011
Mutations at the Base of the Icosahedral Five-Fold Cylinders of Minute Virus of Mice Induce 3′-to-5′ Genome Uncoating and Critically Impair Entry Functions
Cotmore SF, Tattersall P. Mutations at the Base of the Icosahedral Five-Fold Cylinders of Minute Virus of Mice Induce 3′-to-5′ Genome Uncoating and Critically Impair Entry Functions. Journal Of Virology 2011, 86: 69-80. PMID: 22013064, PMCID: PMC3255873, DOI: 10.1128/jvi.06119-11.Peer-Reviewed Original ResearchConceptsSubgenomic DNAWild typeAnalysis of progenyMinute virusVP2 N-terminusDNA genomeAccumulation of virionsUncoating reactionGenome releaseImpaired mutantsEndosomal compartmentsEntry defectN-terminusVirion assemblyMutantsProtein capsidGenome uncoatingCation depletionBilayer penetrationCell entryDNAGenomeVP1 domainTerminusProteolysisStructure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold Axis
Plevka P, Hafenstein S, Li L, D'Abrgamo A, Cotmore SF, Rossmann MG, Tattersall P. Structure of a Packaging-Defective Mutant of Minute Virus of Mice Indicates that the Genome Is Packaged via a Pore at a 5-Fold Axis. Journal Of Virology 2011, 85: 4822-4827. PMID: 21367911, PMCID: PMC3126206, DOI: 10.1128/jvi.02598-10.Peer-Reviewed Original Research
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
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 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 Research
1999
Controlled 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 structureHigh-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 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 Research
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