Cryo-EM Structure of the African Swine Fever Virus

文献类型： 外文期刊

第一作者： Liu, Sheng

作者： Liu, Sheng;Gao, George F.;Liu, Sheng;Li, Shihua;Zhao, Zhennan;Bi, Yuhai;Peng, Ruchao;Sun, Yeping;Qi, Jianxun;Shi, Yi;Gao, George F.;Luo, Yuzi;Sun, Yuan;Li, Su;Zhang, Li;Wang, Wei;Qiu, Hua-Ji;Luo, Yuzi;Sun, Yuan;Li, Su;Zhang, Li;Wang, Wei;Qiu, Hua-Ji;Wang, Yajuan;Zhu, Dongjie;Zhang, Xinzheng;Bi, Yuhai;Shi, Yi;Gao, George F.;Sun, Junqing;Shi, Yi;Wang, Peiyi;Gao, George F.;Song, Hao;Gao, George F.;Shi, Yi;Gao, George F.;Wang, Peiyi;Gao, George F.;Yan, Jinghua

作者机构：

期刊名称：CELL HOST & MICROBE （ 影响因子：21.023； 五年影响因子：22.103 ）

ISSN： 1931-3128

年卷期： 2019 年 26 卷 6 期

页码：

收录情况： SCI

摘要： African swine fever virus (ASFV) is a large double-stranded DNA virus with an icosahedral multilayered structure. ASFV causes a lethal swine hemorrhagic disease and is currently responsible for widespread damage to the pork industry in Asia. Neither vaccines nor antivirals are available and the molecular characterization of the ASFV particle is outstanding. Here, we describe the cryogenic electron microscopy (cryo-EM) structure of the icosahedral capsid of ASFV at 4.6-angstrom. The ASFV particle consists of 8,280 copies of the major capsid protein p72, 60 copies of the penton protein, and at least 8,340 minor capsid proteins, of which there might be 3 different types. Like other nucleocytoplasmic large DNA viruses, the minor capsid proteins form a hexagonal network below the outer capsid shell, functioning as stabilizers by "gluing" neighboring capsomers together. Our findings provide a comprehensive molecular model of the ASFV capsid architecture that will contribute to the future development of countermeasures, including vaccines.

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