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Journal of Virology, August 2006, p. 7625-7635, Vol. 80, No. 15
0022-538X/06/$08.00+0     doi:10.1128/JVI.00522-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Characterization of the Archaeal Thermophile Sulfolobus Turreted Icosahedral Virus Validates an Evolutionary Link among Double-Stranded DNA Viruses from All Domains of Life

Walid S. A. Maaty,¹ Alice C. Ortmann,² Mensur Dlaki,³ Katie Schulstad,¹ Jonathan K. Hilmer,¹ Lars Liepold,¹ Blake Weidenheft,² Reza Khayat,⁴ Trevor Douglas,¹ Mark J. Young,² and Brian Bothner^1*

Department of Chemistry and Biochemistry, Montana State University, Bozeman,¹ Departments of Microbiology and Plant Sciences, Montana State University, Bozeman,² Department of Microbiology, Montana State University, Bozeman, Montana 59717,³ Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037⁴

Received 13 March 2006/ Accepted 17 May 2006

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.

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