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CryoEM structure of the tegumented capsid of Epstein-Barr virus.
Cell Research ( IF 44.1 ) Pub Date : 2020-07-03 , DOI: 10.1038/s41422-020-0363-0
Zhihai Li 1 , Xiao Zhang 2 , Lili Dong 1 , Jingjing Pang 1, 3 , Miao Xu 2 , Qian Zhong 2 , Mu-Sheng Zeng 2 , Xuekui Yu 1, 3
Affiliation  

Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection.



中文翻译:

Epstein-Barr 病毒外被衣壳的 CryoEM 结构。

爱泼斯坦-巴尔病毒 (EBV) 是传染性单核细胞增多症的主要原因,已被证明与各种恶性肿瘤密切相关。在这里,我们提出了一个完整的 EBV 原子模型,包括二十面体衣壳、十二聚体门户和衣壳相关的被覆复合体 (CATC)。我们来自外被衣壳的原位入口采用封闭构象,其通道阀保持末端病毒 DNA,其冠部区域与三层环状 dsDNA 牢固接合,这与五邻体的灵活性一起,有效地减轻了衣壳内部施加在门帽上的压力。相比之下,CATCs 通过以化学计量方式与柔性五邻体顶点结合,准确地增加内衣壳压力,以促进压力驱动的基因组传递。一起,

更新日期:2020-07-03
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