title: Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life.
abstract: Icosahedral nontailed double-stranded DNA (dsDNA) viruses are present in all three domains of life, leading to speculation about a common viral ancestor that predates the divergence of Eukarya, Bacteria, and Archaea. This suggestion is supported by the shared general architecture of this group of viruses and the common fold of their major capsid protein. However, limited information on the diversity and replication of archaeal viruses, in general, has hampered further analysis. Sulfolobus turreted icosahedral virus (STIV), isolated from a hot spring in Yellowstone National Park, was the first icosahedral virus with an archaeal host to be described. Here we present a detailed characterization of the components forming this unusual virus. Using a proteomics-based approach, we identified nine viral and two host proteins from purified STIV particles. Interestingly, one of the viral proteins originates from a reading frame lacking a consensus start site. The major capsid protein (B345) was found to be glycosylated, implying a strong similarity to proteins from other dsDNA viruses. Sequence analysis and structural predication of virion-associated viral proteins suggest that they may have roles in DNA packaging, penton formation, and protein-protein interaction. The presence of an internal lipid layer containing acidic tetraether lipids has also been confirmed. The previously presented structural models in conjunction with the protein, lipid, and carbohydrate information reported here reveal that STIV is strikingly similar to viruses associated with the Bacteria and Eukarya domains of life, further strengthening the hypothesis for a common ancestor of this group of dsDNA viruses from all domains of life.
authors.affiliation: Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59715, USA.
authors.forename: Walid S A
authors.initials: WS
authors.lastname: Maaty
authors.forename: Alice C
authors.initials: AC
authors.lastname: Ortmann
authors.forename: Mensur
authors.initials: M
authors.lastname: Dlakić
authors.forename: Katie
authors.initials: K
authors.lastname: Schulstad
authors.forename: Jonathan K
authors.initials: JK
authors.lastname: Hilmer
authors.forename: Lars
authors.initials: L
authors.lastname: Liepold
authors.forename: Blake
authors.initials: B
authors.lastname: Weidenheft
authors.forename: Reza
authors.initials: R
authors.lastname: Khayat
authors.forename: Trevor
authors.initials: T
authors.lastname: Douglas
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Young
authors.forename: Brian
authors.initials: B
authors.lastname: Bothner
mesh_terms: D000595:Amino Acid Sequence; D023641:Archaeal Viruses / Q000502:physiology*; D005075:Biological Evolution; D002213:Capsid / Q000502:physiology*; D004267:DNA Viruses / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D040901:Proteomics; D017386:Sequence Homology, Amino Acid; D021241:Spectrometry, Mass, Electrospray Ionization; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D016944:Sulfolobus / Q000821:virology*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D014764:Viral Proteins