dc.contributor.author | Laanto, Elina | |
dc.contributor.author | Mäntynen, Sari | |
dc.contributor.author | De Colibus, Luigi | |
dc.contributor.author | Marjakangas, Jenni | |
dc.contributor.author | Gillum, Ashley | |
dc.contributor.author | Stuart, David I. | |
dc.contributor.author | Ravantti, Janne | |
dc.contributor.author | Huiskonen, Juha T. | |
dc.contributor.author | Sundberg, Lotta-Riina | |
dc.date.accessioned | 2017-11-16T10:45:23Z | |
dc.date.available | 2017-11-16T10:45:23Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | Laanto, 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.other | CONVID_27124298 | |
dc.identifier.other | TUTKAID_74475 | |
dc.identifier.uri | https://jyx.jyu.fi/handle/123456789/55902 | |
dc.description.abstract | Viruses 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.iso | eng | |
dc.publisher | National Academy of Sciences | |
dc.relation.ispartofseries | Proceedings of the National Academy of Sciences of the United States of America | |
dc.subject.other | cryo-electron microscopy | |
dc.subject.other | Flavobacterium | |
dc.subject.other | structure | |
dc.title | Virus found in a boreal lake links ssDNA and dsDNA viruses | |
dc.type | article | |
dc.identifier.urn | URN:NBN:fi:jyu-201711154261 | |
dc.contributor.laitos | Bio- ja ympäristötieteiden laitos | fi |
dc.contributor.laitos | Department of Biological and Environmental Science | en |
dc.contributor.oppiaine | Solu- ja molekyylibiologia | fi |
dc.contributor.oppiaine | Biologisten vuorovaikutusten huippututkimusyksikkö | fi |
dc.contributor.oppiaine | Nanoscience Center | fi |
dc.contributor.oppiaine | Cell and Molecular Biology | en |
dc.contributor.oppiaine | Centre of Excellence in Biological Interactions Research | en |
dc.contributor.oppiaine | Nanoscience Center | en |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | |
dc.date.updated | 2017-11-15T13:15:09Z | |
dc.type.coar | http://purl.org/coar/resource_type/c_2df8fbb1 | |
dc.description.reviewstatus | peerReviewed | |
dc.format.pagerange | 8378-8383 | |
dc.relation.issn | 0027-8424 | |
dc.relation.numberinseries | 31 | |
dc.relation.volume | 114 | |
dc.type.version | acceptedVersion | |
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.accesslevel | openAccess | fi |
dc.relation.grantnumber | 266879 | |
dc.subject.yso | lipidit | |
dc.subject.yso | perimä | |
dc.subject.yso | virukset | |
dc.subject.yso | järvet | |
dc.subject.yso | boreaalinen vyöhyke | |
dc.subject.yso | bakteriofagit | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p4799 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p8862 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p1123 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p9374 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p16692 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p25303 | |
dc.relation.doi | 10.1073/pnas.1703834114 | |
dc.relation.funder | Suomen Akatemia | fi |
dc.relation.funder | Research Council of Finland | en |
jyx.fundingprogram | Akatemiatutkija, SA | fi |
jyx.fundingprogram | Academy Research Fellow, AoF | en |
jyx.fundinginformation | This 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.okm | A1 | |