Identification of Capsid/Coat Related Protein Folds and Their Utility for Virus Classification.

Identification of Capsid/Coat Related Protein Folds and Their Utility for Virus Classification.
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DOI:
10.3389/fmicb.2017.00380
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发表时间:
2017
影响因子:
5.2
通讯作者:
Caetano-Anollés G
Caetano-Anollés G
中科院分区:
生物学2区
文献类型:
--
作者:
Nasir A;Caetano-Anollés G

文献摘要

被引文献

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病毒超级组包括漫游在我们的星球上并感染生命形式的已知和未知病毒的全部集合。超类群在遗传学和形态学上都非常多样化,历史上一直难以研究和分类。过去几年蛋白质结构数据的积累为重新审视病毒的分类和进化提供了极好的机会。在这里,我们扫描完全测序的病毒蛋白质组从所有基因组类型,并确定蛋白质折叠参与病毒衣壳和病毒粒子结构的形成。在对已发表的文献进行基准测试后,将编码类似衣壳/外壳相关折叠的病毒合并成谱系。值得注意的是,计算机模拟实验重现了所有先前描述的已知基于结构的病毒谱系的成员,沿着了几个新添加的提议,这表明它可能是实验方法的有用补充,并有助于宏基因组样品中病毒多样性的定性评估。
The viral supergroup includes the entire collection of known and unknown viruses that roam our planet and infect life forms. The supergroup is remarkably diverse both in its genetics and morphology and has historically remained difficult to study and classify. The accumulation of protein structure data in the past few years now provides an excellent opportunity to re-examine the classification and evolution of viruses. Here we scan completely sequenced viral proteomes from all genome types and identify protein folds involved in the formation of viral capsids and virion architectures. Viruses encoding similar capsid/coat related folds were pooled into lineages, after benchmarking against published literature. Remarkably, the in silico exercise reproduced all previously described members of known structure-based viral lineages, along with several proposals for new additions, suggesting it could be a useful supplement to experimental approaches and to aid qualitative assessment of viral diversity in metagenome samples.