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 Research
2011
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
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
1999
cis 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 lengthVectorControlled 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 ResearchConceptsAmino 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
1992
In 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 ResearchTwo 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 cellsThe 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 cellsIn vivo resolution of circular plasmids containing concatemer junction fragments from minute virus of mice DNA and their subsequent replication as linear molecules
Cotmore S, Tattersall P. In vivo resolution of circular plasmids containing concatemer junction fragments from minute virus of mice DNA and their subsequent replication as linear molecules. Journal Of Virology 1992, 66: 420-431. PMID: 1530771, PMCID: PMC238302, DOI: 10.1128/jvi.66.1.420-431.1992.Peer-Reviewed Original Research
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 characteristicsSusceptibility of human cells to killing by the parvoviruses H-1 and minute virus of mice correlates with viral transcription
Cornelis J, Chen Y, Spruyt N, Duponchel N, Cotmore S, Tattersall P, Rommelaere J. Susceptibility of human cells to killing by the parvoviruses H-1 and minute virus of mice correlates with viral transcription. Journal Of Virology 1990, 64: 2537-2544. PMID: 2139892, PMCID: PMC249429, DOI: 10.1128/jvi.64.6.2537-2544.1990.Peer-Reviewed Original ResearchConceptsViral mRNAsHuman cellsLevel of transcriptionMinute virusMajor viral transcriptViral DNA amplificationNonstructural polypeptidesGene productsOncogenic transformationGene expressionIntracellular localizationNonstructural proteinsViral transcriptionViral transcriptsTranscriptionViral genomeParvovirus HCell susceptibilityHuman fibroblastsVirus uptakeEpithelial cellsDNA amplificationResistant derivativesKeratinocyte lineDifferential susceptibility
1989
A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles
Cotmore S, Tattersall P. A genome-linked copy of the NS-1 polypeptide is located on the outside of infectious parvovirus particles. Journal Of Virology 1989, 63: 3902-3911. PMID: 2527311, PMCID: PMC250986, DOI: 10.1128/jvi.63.9.3902-3911.1989.Peer-Reviewed Original ResearchConceptsNS-1 moleculesHost cellsSingle-strand DNA genomeNonstructural protein NS-1Amino-terminal domainNew host cellsNS-1 polypeptideAutonomous parvovirus minute virusParvovirus minute virusNS-1Normal culture conditionsDNA genomeS2 formA9 cellsLimited proteolysisIncoming virusMinute virusProteolytic digestionDNADNA coreMost virionsCulture conditionsVirionsPolypeptideParvovirus particlesLimitations to the expression of parvoviral nonstructural proteins may determine the extent of sensitization of EJ-ras-transformed rat cells to minute virus of mice
Van Hille B, Duponchel N, Salomé N, Spruyt N, Cotmore S, Tattersall P, Cornelis J, Rommelaere J. Limitations to the expression of parvoviral nonstructural proteins may determine the extent of sensitization of EJ-ras-transformed rat cells to minute virus of mice. Virology 1989, 171: 89-97. PMID: 2525841, DOI: 10.1016/0042-6822(89)90514-x.Peer-Reviewed Original ResearchConceptsNonstructural proteinsNonstructural protein NS-1Parvoviral DNA replicationRat cellsParvoviral life cycleNonstructural viral proteinsDNA replicationRat cell linesSensitivity of cellsRas transformationP21ras proteinsNormal rat cellsGene expressionMVMp infectionParvovirus MVMpNRK cellsViral proteinsEarly blockProteinCell linesViral DNALife cycleNS-1MVMpExpression
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
1986
Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments
Cotmore S, McKie V, Anderson L, Astell C, Tattersall P. Identification of the major structural and nonstructural proteins encoded by human parvovirus B19 and mapping of their genes by procaryotic expression of isolated genomic fragments. Journal Of Virology 1986, 60: 548-557. PMID: 3021988, PMCID: PMC288924, DOI: 10.1128/jvi.60.2.548-557.1986.Peer-Reviewed Original ResearchConceptsProtein sequencesViral capsid polypeptidesCapsid polypeptidesSucrose velocity gradientsB19 genomeBacterial plasmid vectorRestriction endonuclease fragmentsGenomic fragmentProtein speciesApparent molecular weightNonstructural polypeptidesExpression constructsSimilar proteinsBAL-31GenomeExpression vectorNonstructural proteinsEndonuclease fragmentsPlasmid vectorViral genomeViral polypeptidesPolypeptide fragmentsProcaryotic expressionPolypeptideProtein
1983
The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides
Cotmore S, Sturzenbecker L, Tattersall P. The autonomous parvovirus MVM encodes two nonstructural proteins in addition to its capsid polypeptides. Virology 1983, 129: 333-343. PMID: 6623929, DOI: 10.1016/0042-6822(83)90172-1.Peer-Reviewed Original ResearchConceptsParvovirus MVMCapsid polypeptidesNS-1 proteinOpen reading frameNS-1 polypeptidePeptide map analysisMajor intronTranscription unitMVM genomeVitro translationApparent molecular weightReading frameNonstructural proteinsPolypeptideProteinVP-1NS-1VP-2GenomeIntronsComigratesMolecular weightTranscriptsMVMMap analysisInteraction of minute virus of mice with differentiated cells: strain-dependent target cell specificity is mediated by intracellular factors
Spalholz B, Tattersall P. Interaction of minute virus of mice with differentiated cells: strain-dependent target cell specificity is mediated by intracellular factors. Journal Of Virology 1983, 46: 937-943. PMID: 6602221, PMCID: PMC256568, DOI: 10.1128/jvi.46.3.937-943.1983.Peer-Reviewed Original ResearchConceptsVirus-host cell interactionsTarget cell specificityCell typesIntracellular host factorsRestrictive cell typesRestrictive infectionCell interactionsMinute virusCell specificityHost cell typesViral determinantsViral replicationSpecific receptorsImmunosuppressive strainHost factorsSame receptorViral DNA synthesisPrototype strainVirusDetectable expressionIncoming viral genomesEarly eventsFinal outcomeInfectionMice
1977
Sequence homology between the structural polypeptides of minute virus of mice
Tattersall P, Shatkin A, Ward D. Sequence homology between the structural polypeptides of minute virus of mice. Journal Of Molecular Biology 1977, 111: 375-394. PMID: 864702, DOI: 10.1016/s0022-2836(77)80060-0.Peer-Reviewed Original ResearchConceptsA polypeptideEmpty virionsPolypeptide BTotal virion proteinsMinute virusPolypeptide speciesB polypeptidesSequence homologyPrecursor-product relationshipVirion proteinsC polypeptideStructural polypeptidesPolypeptideCommon sequenceEmpty particlesVirionsProteinDifferent conformationsEnzymePrevious kinetic studiesSequenceVivo observationsCleavageConformationVivo