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dc.contributor.authorLaanto, Elina
dc.contributor.authorMäntynen, Sari
dc.contributor.authorDe Colibus, Luigi
dc.contributor.authorMarjakangas, Jenni
dc.contributor.authorGillum, Ashley
dc.contributor.authorStuart, David I.
dc.contributor.authorRavantti, Janne
dc.contributor.authorHuiskonen, Juha T.
dc.contributor.authorSundberg, Lotta-Riina
dc.date.accessioned2017-11-16T10:45:23Z
dc.date.available2017-11-16T10:45:23Z
dc.date.issued2017
dc.identifier.citationLaanto, E., Mäntynen, S., De Colibus, L., Marjakangas, J., Gillum, A., Stuart, D. I., Ravantti, J., Huiskonen, J. T., & Sundberg, L.-R. (2017). Virus found in a boreal lake links ssDNA and dsDNA viruses. <i>Proceedings of the National Academy of Sciences of the United States of America</i>, <i>114</i>(31), 8378-8383. <a href="https://doi.org/10.1073/pnas.1703834114" target="_blank">https://doi.org/10.1073/pnas.1703834114</a>
dc.identifier.otherCONVID_27124298
dc.identifier.otherTUTKAID_74475
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/55902
dc.description.abstractViruses have impacted the biosphere in numerous ways since the dawn of life. However, the evolution, genetic, structural, and taxonomic diversity of viruses remain poorly understood, in part because sparse sampling of the virosphere has concentrated mostly on exploring the abundance and diversity of dsDNA viruses. Furthermore, viral genomes are highly diverse, and using only the current sequence-based methods for classifying viruses and studying their phylogeny is complicated. Here we describe a virus, FLiP (Flavobacterium-infecting, lipid-containing phage), with a circular ssDNA genome and an internal lipid membrane enclosed in the icosahedral capsid. The 9,174-nt-long genome showed limited sequence similarity to other known viruses. The genetic data imply that this virus might use replication mechanisms similar to those found in other ssDNA replicons. However, the structure of the viral major capsid protein, elucidated at near-atomic resolution using cryo-electron microscopy, is strikingly similar to that observed in dsDNA viruses of the PRD1–adenovirus lineage, characterized by a major capsid protein bearing two β-barrels. The strong similarity between FLiP and another member of the structural lineage, bacteriophage PM2, extends to the capsid organization (pseudo T = 21 dextro) despite the difference in the genetic material packaged and the lack of significant sequence similarity.
dc.language.isoeng
dc.publisherNational Academy of Sciences
dc.relation.ispartofseriesProceedings of the National Academy of Sciences of the United States of America
dc.subject.othercryo-electron microscopy
dc.subject.otherFlavobacterium
dc.subject.otherstructure
dc.titleVirus found in a boreal lake links ssDNA and dsDNA viruses
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201711154261
dc.contributor.laitosBio- ja ympäristötieteiden laitosfi
dc.contributor.laitosDepartment of Biological and Environmental Scienceen
dc.contributor.oppiaineSolu- ja molekyylibiologiafi
dc.contributor.oppiaineBiologisten vuorovaikutusten huippututkimusyksikköfi
dc.contributor.oppiaineNanoscience Centerfi
dc.contributor.oppiaineCell and Molecular Biologyen
dc.contributor.oppiaineCentre of Excellence in Biological Interactions Researchen
dc.contributor.oppiaineNanoscience Centeren
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2017-11-15T13:15:09Z
dc.type.coarhttp://purl.org/coar/resource_type/c_2df8fbb1
dc.description.reviewstatuspeerReviewed
dc.format.pagerange8378-8383
dc.relation.issn0027-8424
dc.relation.numberinseries31
dc.relation.volume114
dc.type.versionacceptedVersion
dc.rights.copyright© the Authors, 2017. This is a final draft version of an article whose final and definitive form has been published by National Academy of Sciences. Published in this repository with the kind permission of the publisher.
dc.rights.accesslevelopenAccessfi
dc.relation.grantnumber266879
dc.subject.ysolipidit
dc.subject.ysoperimä
dc.subject.ysovirukset
dc.subject.ysojärvet
dc.subject.ysoboreaalinen vyöhyke
dc.subject.ysobakteriofagit
jyx.subject.urihttp://www.yso.fi/onto/yso/p4799
jyx.subject.urihttp://www.yso.fi/onto/yso/p8862
jyx.subject.urihttp://www.yso.fi/onto/yso/p1123
jyx.subject.urihttp://www.yso.fi/onto/yso/p9374
jyx.subject.urihttp://www.yso.fi/onto/yso/p16692
jyx.subject.urihttp://www.yso.fi/onto/yso/p25303
dc.relation.doi10.1073/pnas.1703834114
dc.relation.funderSuomen Akatemiafi
dc.relation.funderResearch Council of Finlanden
jyx.fundingprogramAkatemiatutkija, SAfi
jyx.fundingprogramAcademy Research Fellow, AoFen
jyx.fundinginformationThis work was supported by the Academy of Finland Center of Excellence Program in Biological Interactions 2012–2017 Grant 252411, by Academy of Finland Grant 266879 (to L.-R.S.), by the Jane and Aatos Erkko Foundation, by Medical Research Council Grant MR/N00065X/1 (to D.I.S.), and by the European Research Council under the European Union’s Horizon 2020 Research and Innovation Programme Grant 649053 (to J.T.H.). A.G. is supported by Wellcome Trust 4-y PhD Studentship 106274/Z/14/Z. The Oxford Particle Imaging Centre was founded by Wellcome Trust Joint Infrastructure Fund Award 060208/Z/00/Z and is supported by Welcome Trust Equipment Grant 093305/Z/10/Z. The Wellcome Trust Centre for Human Genetics is supported by Wellcome Trust Centre Grant 090532/Z/09/Z.
dc.type.okmA1


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