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Virus found in a boreal lake links ssDNA and dsDNA viruses

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Laanto, E., Mäntynen, S., De Colibus, L., Marjakangas, J., Gillum, A., Stuart, D. I., . . . Sundberg, L.-R. (2017). Virus found in a boreal lake links ssDNA and dsDNA viruses. Proceedings of the National Academy of Sciences of the United States of America, 114 (31), 8378-8383. doi:10.1073/pnas.1703834114
Published in
Proceedings of the National Academy of Sciences of the United States of America
Authors
Laanto, Elina |
Mäntynen, Sari |
De Colibus, Luigi |
Marjakangas, Jenni |
Gillum, Ashley |
Stuart, David I. |
Ravantti, Janne |
Huiskonen, Juha T. |
Sundberg, Lotta-Riina
Date
2017
Discipline
Solu- ja molekyylibiologia
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.

 
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. ...
Publisher
National Academy of Sciences
ISSN Search the Publication Forum
0027-8424
Keywords
virukset bakteriofagit perimä järvet boreaalinen vyöhyke cryo-electron microscopy Flavobacterium lipids genome structure
DOI
https://doi.org/10.1073/pnas.1703834114
URI

http://urn.fi/URN:NBN:fi:jyu-201711154261

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