Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life
Characterization of the archaeal thermophile Sulfolobus turreted icosahedral virus validates an evolutionary link among double-stranded DNA viruses from all domains of life
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DOI：
10.1128/jvi.00522-06
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发表时间：
2006-08-01
影响因子：
5.4
通讯作者：
Bothner, Brian
中科院分区：
文献类型：
--
作者：
Maaty, Walid S. A.;Ortmann, Alice C.;Bothner, Brian
二十面体无尾双链DNA（dsDNA）病毒存在于生命的所有三个领域，导致人们猜测在真核生物，细菌和细菌的分歧之前有一个共同的病毒祖先。这组病毒共有的一般结构和它们的主要衣壳蛋白的共同折叠支持这一建议。然而，关于古细菌病毒的多样性和复制的信息有限，一般来说，阻碍了进一步的分析。从黄石国家公园的一个温泉中分离到的苏菲洛布斯塔状二十面体病毒（Suffiblobus turreted icosahedral virus，STIV）是第一个被描述的具有古细菌宿主的二十面体病毒。在这里，我们提出了一个详细的组成部分，形成这种不寻常的病毒的特性。使用蛋白质组学为基础的方法，我们确定了九个病毒和两个主机蛋白纯化的STIV颗粒。有趣的是，其中一种病毒蛋白来源于缺乏共有起始位点的阅读框架。发现主要衣壳蛋白（B345）是糖基化的，这意味着与其他dsDNA病毒的蛋白质具有很强的相似性。病毒粒子相关蛋白的序列分析和结构预测表明，它们可能在DNA包装、五邻体形成和蛋白质-蛋白质相互作用中发挥作用。含有酸性四醚脂质的内部脂质层的存在也已得到证实。先前提出的结构模型结合蛋白质，脂质和碳水化合物的信息在这里报告显示，STIV是惊人的相似，与细菌和真核生物领域的生活，进一步加强了这组dsDNA病毒的共同祖先的假设，从所有领域的生活。
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. Suffiblobus 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.