6533b857fe1ef96bd12b3d05

RESEARCH PRODUCT

Virus found in a boreal lake links ssDNA and dsDNA viruses.

Janne J. RavanttiJanne J. RavanttiSari MäntynenElina LaantoLotta-riina SundbergJenni MarjakangasJuha T. HuiskonenJuha T. HuiskonenDavid I. StuartLuigi De ColibusAshley Gillum

subject

0301 basic medicineBACTERIALviruksetProtein ConformationviruseslipiditGenomechemistry.chemical_compoundProtein structureBINDINGVIRAL UNIVERSE1183 Plant biology microbiology virologyGeneticsMultidisciplinaryCRYOELECTRON MICROSCOPYBiological Sciencesboreaalinen vyöhykeCapsidViral evolutionCAPSID PROTEINLineage (genetic)030106 microbiologyGENOMESDNA Single-Strandedcryo-electron microscopyGenome ViralBiologyPROTEIN STRUCTURESjärvetFlavobacteriumVirusbakteriofagitlipids03 medical and health sciencesCapsidPhylogeneticsBacteriophage PRD1structuregenometa1182DNA VirusesDNAEVOLUTIONLakes030104 developmental biologychemistryperimäCapsid ProteinsCOMMUNITIESDNA

description

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 beta-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. Peer reviewed

10.1073/pnas.1703834114https://pubmed.ncbi.nlm.nih.gov/28716906