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ShanghaiTech University Knowledge Management System
Cryo-EM structure of a herpesvirus capsid at 3.1 angstrom | |
2018-04-06 | |
发表期刊 | SCIENCE (IF:44.7[JCR-2023],50.3[5-Year]) |
ISSN | 0036-8075 |
卷号 | 360期号:6384页码:48-+ |
发表状态 | 已发表 |
DOI | 10.1126/science.aao7283 |
摘要 | Structurally and genetically, human herpesviruses are among the largest and most complex of viruses. Using cryo-electron microscopy (cryo-EM) with an optimized image reconstruction strategy, we report the herpes simplex virus type 2 (HSV-2) capsid structure at 3.1 angstroms, which is built up of about 3000 proteins organized into three types of hexons (central, peripentonal, and edge), pentons, and triplexes. Both hexons and pentons contain the major capsid protein, VP5; hexons also contain a small capsid protein, VP26; and triplexes comprise VP23 and VP19C. Acting as core organizers, VP5 proteins form extensive intermolecular networks, involving multiple disulfide bonds (about 1500 in total) and noncovalent interactions, with VP26 proteins and triplexes that underpin capsid stability and assembly. Conformational adaptations of these proteins induced by their microenvironments lead to 46 different conformers that assemble into a massive quasisymmetric shell, exemplifying the structural and functional complexity of HSV. |
收录类别 | SCI ; SCIE |
语种 | 英语 |
资助项目 | Natural Science Foundation of Hunan Province[2017RS3033] |
WOS研究方向 | Science & Technology - Other Topics |
WOS类目 | Multidisciplinary Sciences |
WOS记录号 | WOS:000429263100042 |
出版者 | AMER ASSOC ADVANCEMENT SCIENCE |
WOS关键词 | SIMPLEX-VIRUS TYPE-1 ; RECOMBINANT BACULOVIRUSES ; SCAFFOLDING PROTEINS ; IN-VITRO ; DNA ; STABILITY ; TRIPLEX ; RECONSTITUTION ; IDENTIFICATION ; VISUALIZATION |
原始文献类型 | Article |
引用统计 | 正在获取...
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文献类型 | 期刊论文 |
条目标识符 | https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/20216 |
专题 | 免疫化学研究所_特聘教授组_饶子和组 |
通讯作者 | Wang, Jialing; Wang, Junzhi; Zhang, Xinzheng; Liu, Hongrong; Rao, Zihe; Wang, Xiangxi |
作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Macromol, Beijing 100101, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Hunan Normal Univ, Coll Phys & Informat Sci, Synerget Innovat Ctr Quantum Effects & Applicat, Changsha 410081, Hunan, Peoples R China 4.Natl Inst Food & Drug Control, 2 Tiantanxili, Beijing 100050, Peoples R China 5.Sinovac Biotech Co Ltd, Beijing 100085, Peoples R China 6.Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China 7.ShanghaiTech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai 201210, Peoples R China 8.Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300353, Peoples R China 9.Tsinghua Univ, Sch Med, Lab Struct Biol, Beijing 100084, Peoples R China |
通讯作者单位 | 免疫化学研究所 |
推荐引用方式 GB/T 7714 | Yuan, Shuai,Wang, Jialing,Zhu, Dongjie,et al. Cryo-EM structure of a herpesvirus capsid at 3.1 angstrom[J]. SCIENCE,2018,360(6384):48-+. |
APA | Yuan, Shuai.,Wang, Jialing.,Zhu, Dongjie.,Wang, Nan.,Gao, Qiang.,...&Wang, Xiangxi.(2018).Cryo-EM structure of a herpesvirus capsid at 3.1 angstrom.SCIENCE,360(6384),48-+. |
MLA | Yuan, Shuai,et al."Cryo-EM structure of a herpesvirus capsid at 3.1 angstrom".SCIENCE 360.6384(2018):48-+. |
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