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
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
The 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
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
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
1986
Organization of nonstructural genes of the autonomous parvovirus minute virus of mice
Cotmore S, Tattersall P. Organization of nonstructural genes of the autonomous parvovirus minute virus of mice. Journal Of Virology 1986, 58: 724-732. PMID: 2939261, PMCID: PMC252977, DOI: 10.1128/jvi.58.3.724-732.1986.Peer-Reviewed Original ResearchConceptsOpen reading frameAutonomous parvovirus minute virusParvovirus minute virusSimilar proteinsFusion proteinCommon amino-terminal sequenceSingle open reading frameNonstructural protein NS-1Rabbit reticulocyte lysate translation systemViral genomeReticulocyte lysate translation systemAlternative open reading framesNS-2 proteinsCarboxy-terminal halfNS-1 proteinNS-1Amino acid sequenceBacterial fusion proteinLysate translation systemMinute virusAmino-terminal sequenceProcaryotic expression vectorR2 transcriptsReading frameAcid sequenceNucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis
Shade R, Blundell M, Cotmore S, Tattersall P, Astell C. Nucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis. Journal Of Virology 1986, 58: 921-936. PMID: 3701931, PMCID: PMC253001, DOI: 10.1128/jvi.58.3.921-936.1986.Peer-Reviewed Original ResearchConceptsNucleotide sequenceLarge open reading frameMajor nonstructural proteinOpen reading frameFull-length cloneMajor structural polypeptidesGenome organizationGenomic clonesPutative polypeptideTranscription unitEntire genomeReading frameDNA sequencesFourth promoterParvovirus genomeSequence informationNonstructural proteinsGenomeTerminal repeatDependovirus genusStructural polypeptidesViral DNAB19 genomePolypeptideSequence