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Virus found in a boreal lake links ssDNA and dsDNA viruses

DOI: 10.1073/pnas.1703834114 DOI Help

Authors: Elina Laanto (University of Jyväskylä) , Sari Mäntynen (University of Jyväskylä) , Luigi De Colibus (Welcome Trust Centre for Human Genetics, University of Oxford) , Jenni Marjakangas (University of Jyväskylä) , Ashley Gillum (Welcome Trust Centre for Human Genetics, University of Oxford) , David I. Stuart (Diamond Light Source) , Janne J. Ravantti (University of Jyväskylä) , Juha Huiskonen (Welcome Trust Centre for Human Genetics, University of Oxford; University of Helsinki) , Lotta-riina Sundberg (University of Jyväskylä)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Proceedings Of The National Academy Of Sciences , VOL 1768

State: Published (Approved)
Published: July 2017

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.

Journal Keywords: cryo-electron microscopy; Flavobacterium; lipids; genome; structure

Subject Areas: Biology and Bio-materials


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Added On: 20/07/2017 14:55

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