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-Å. 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.

非洲猪瘟病毒（ASFV）是具有二十面体多层结构的大型双链DNA病毒。ASFV引起致命的猪出血性疾病，目前对亚洲猪肉业造成广泛破坏。既没有疫苗也没有抗病毒药，并且ASFV颗粒的分子表征非常出色。在这里，我们描述了ASFV的二十面体衣壳在4.6-Å处的低温电子显微镜（cryo-EM）结构。ASFV颗粒由8,280拷贝的主要衣壳蛋白p72、60拷贝的戊糖蛋白和至少8,340个次要衣壳蛋白组成，其中可能有3种不同类型。像其他核质大DNA病毒一样，次要衣壳蛋白在衣壳外层下方形成一个六边形网络，通过将相邻的衣藻头“胶合”在一起，起到稳定剂的作用。我们的发现提供了ASFV衣壳结构的全面分子模型，这将有助于未来对策的发展，包括疫苗。