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DOI | 10.1126/science.aaz1439 |
Architecture of African swine fever virus and implications for viral assembly | |
Wang, Nan1,2; Zhao, Dongming3,4; Wang, Jialing1,2; Zhang, Yangling1,2; Wang, Ming3,4; Gao, Yan5,6,7; Li, Fang3,4; Wang, Jingfei3,4; Bu, Zhigao3,4; Rao, Zihe1,5,6,7,8; Wang, Xiangxi1,2 | |
2019-11-01 | |
发表期刊 | SCIENCE
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ISSN | 0036-8075 |
EISSN | 1095-9203 |
出版年 | 2019 |
卷号 | 366期号:6465页码:640-+ |
文章类型 | Article |
语种 | 英语 |
国家 | Peoples R China |
英文摘要 | 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. |
领域 | 地球科学 ; 气候变化 ; 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000494465700050 |
WOS关键词 | PROTEINS ; MEMBRANE ; INSIGHTS ; ANTIBODIES |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://119.78.100.173/C666/handle/2XK7JSWQ/226135 |
专题 | 环境与发展全球科技态势 |
作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Macromol, CAS Key Lab Infect & Immun, Beijing 100101, Peoples R China; 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China; 3.Chinese Acad Agr Sci, Harbin Vet Res Inst, State Key Lab Vet Biotechnol, Harbin 150069, Heilongjiang, Peoples R China; 4.Chinese Acad Agr Sci, Harbin Vet Res Inst, Natl High Containment Lab Anim Dis Control & Prev, Harbin 150069, Heilongjiang, Peoples R China; 5.ShanghaiTech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai 201210, Peoples R China; 6.ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China; 7.Tsinghua Univ, Sch Med, Lab Struct Biol, Beijing 100084, Peoples R China; 8.Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300353, Peoples R China |
推荐引用方式 GB/T 7714 | Wang, Nan,Zhao, Dongming,Wang, Jialing,et al. Architecture of African swine fever virus and implications for viral assembly[J]. SCIENCE,2019,366(6465):640-+. |
APA | Wang, Nan.,Zhao, Dongming.,Wang, Jialing.,Zhang, Yangling.,Wang, Ming.,...&Wang, Xiangxi.(2019).Architecture of African swine fever virus and implications for viral assembly.SCIENCE,366(6465),640-+. |
MLA | Wang, Nan,et al."Architecture of African swine fever virus and implications for viral assembly".SCIENCE 366.6465(2019):640-+. |
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