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Science. 2019 Nov 1;366(6465):640-644. doi: 10.1126/science.aaz1439. Epub 2019 Oct 17.

Architecture of African swine fever virus and implications for viral assembly.

Wang N1,2, Zhao D3, Wang J1,2, Zhang Y1,2, Wang M3, Gao Y4,5, Li F3, Wang J3, Bu Z6, Rao Z7,4,5,8, Wang X7,2.

Author information

1
CAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
2
University of Chinese Academy of Sciences, Beijing 100049, China.
3
State Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.
4
Shanghai Institute for Advanced Immunochemical Studies and School of Life Science and Technology, ShanghaiTech University, Shanghai 201210, China.
5
Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, China.
6
State Key Laboratory of Veterinary Biotechnology and National High Containment Laboratory for Animal Diseases Control and Prevention, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China. xiangxi@ibp.ac.cn buzhigao@caas.cn raozh@tsinghua.edu.cn.
7
CAS Key Laboratory of Infection and Immunity, National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. xiangxi@ibp.ac.cn buzhigao@caas.cn raozh@tsinghua.edu.cn.
8
State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300353, China.

Abstract

African swine fever virus (ASFV) is a giant and complex DNA virus that causes a highly contagious and often lethal swine disease for which no vaccine is available. Using an optimized image reconstruction strategy, we solved the ASFV capsid structure up to 4.1 angstroms, which is built from 17,280 proteins, including one major (p72) and four minor (M1249L, p17, p49, and H240R) capsid proteins organized into pentasymmetrons and trisymmetrons. The atomic structure of the p72 protein informs putative conformational epitopes, distinguishing ASFV from other nucleocytoplasmic large DNA viruses. The minor capsid proteins form a complicated network below the outer capsid shell, stabilizing the capsid by holding adjacent capsomers together. Acting as core organizers, 100-nanometer-long M1249L proteins run along each edge of the trisymmetrons that bridge two neighboring pentasymmetrons and form extensive intermolecular networks with other capsid proteins, driving the formation of the capsid framework. These structural details unveil the basis of capsid stability and assembly, opening up new avenues for African swine fever vaccine development.

PMID:
31624094
DOI:
10.1126/science.aaz1439

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