Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus
文献类型：期刊论文
| 作者 | Li, Zhihai3,4,5; Pang, Jingjing2,3,4; Gao, Rongchao4; Wang, Qingxia4; Zhang, Maoyan1; Yu, Xuekui1,2,3,4
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| 刊名 | NATURE COMMUNICATIONS
 |
| 出版日期 | 2023-04-11 |
| 卷号 | 14期号:1页码:2025 |
| DOI | 10.1038/s41467-023-37779-0 |
| 文献子类 | Article |
| 英文摘要 | Scientists revealed how scaffold of HCMV capsid binds to portal and how the portal undergoes conformational changes as DNA package proceeds. These findings advanced understanding of the mechanism for capsid assembly and maturation in herpesviruses. The portal-scaffold complex is believed to nucleate the assembly of herpesvirus procapsids. During capsid maturation, two events occur: scaffold expulsion and DNA incorporation. The portal-scaffold interaction and the conformational changes that occur to the portal during the different stages of capsid formation have yet to be elucidated structurally. Here we present high-resolution structures of the A- and B-capsids and in-situ portals of human cytomegalovirus. We show that scaffolds bind to the hydrophobic cavities formed by the dimerization and Johnson-fold domains of the major capsid proteins. We further show that 12 loop-helix-loop fragments-presumably from the scaffold domain-insert into the hydrophobic pocket of the portal crown domain. The portal also undergoes significant changes both positionally and conformationally as it accompanies DNA packaging. These findings unravel the mechanism by which the portal interacts with the scaffold to nucleate capsid assembly and further our understanding of scaffold expulsion and DNA incorporation. |
| WOS关键词 | HERPES-SIMPLEX-VIRUS ; SCAFFOLDING PROTEIN ; N-TERMINUS ; IDENTIFICATION ; FEATURES ; TYPE-1 ; DOMAIN ; CELLS ; INFECTION ; VERTEX |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:001166947800018 |
| 出版者 | NATURE PORTFOLIO |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/309645]  |
| 专题 | 新药研究国家重点实验室 |
| 通讯作者 | Yu, Xuekui |
| 作者单位 | 1.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Jiangsu, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China; 3.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China; 4.Chinese Acad Sci, Cryoelect Microscopy Res Ctr, Shanghai 201203, Peoples R China; 5.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Hangzhou 310024, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Li, Zhihai,Pang, Jingjing,Gao, Rongchao,et al. Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus[J]. NATURE COMMUNICATIONS,2023,14(1):2025. |
| APA | Li, Zhihai,Pang, Jingjing,Gao, Rongchao,Wang, Qingxia,Zhang, Maoyan,&Yu, Xuekui.(2023).Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus.NATURE COMMUNICATIONS,14(1),2025. |
| MLA | Li, Zhihai,et al."Cryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus".NATURE COMMUNICATIONS 14.1(2023):2025. |
入库方式： OAI收割
来源：上海药物研究所
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