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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])
ISSN0036-8075
卷号360期号:6384页码:48-+
发表状态已发表
DOI10.1126/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
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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
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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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