Global S&T Development Trend Analysis Platform of Resources and Environment
DOI | 10.1038/ncomms14595 |
The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins | |
El Omari, Kamel1,2; Li, Sai1,9; Kotecha, Abhay1; Walter, Thomas S.1; Bignon, Eduardo A.3; Harlos, Karl1; Somerharju, Pentti4; De Haas, Felix5; Clare, Daniel K.2; Molin, Mika6; Hurtado, Felipe3; Li, Mengqiu1; Grimes, Jonathan M.1,2; Bamford, Dennis H.7; Tischler, Nicole D.3; Huiskonen, Juha T.1,7,8; Stuart, David I.1,2; Roine, Elina7 | |
2019-02-19 | |
发表期刊 | NATURE COMMUNICATIONS
![]() |
ISSN | 2041-1723 |
出版年 | 2019 |
卷号 | 10 |
文章类型 | Article |
语种 | 英语 |
国家 | England; Chile; Finland; Netherlands; Peoples R China |
英文摘要 | Lipid membrane fusion is an essential function in many biological processes. Detailed mechanisms of membrane fusion and the protein structures involved have been mainly studied in eukaryotic systems, whereas very little is known about membrane fusion in prokaryotes. Haloarchaeal pleomorphic viruses (HRPVs) have a membrane envelope decorated with spikes that are presumed to be responsible for host attachment and membrane fusion. Here we determine atomic structures of the ectodomains of the 57-kDa spike protein VP5 from two related HRPVs revealing a previously unreported V-shaped fold. By Volta phase plate cryo-electron tomography we show that VP5 is monomeric on the viral surface, and we establish the orientation of the molecules with respect to the viral membrane. We also show that the viral membrane fuses with the host cytoplasmic membrane in a process mediated by VP5. This sheds light on protein structures involved in prokaryotic membrane fusion. |
领域 | 资源环境 |
收录类别 | SCI-E |
WOS记录号 | WOS:000459056400003 |
WOS关键词 | NANOLITRE CRYSTALLIZATION EXPERIMENTS ; INFLUENZA-VIRUS ; SYSTEM ; VISUALIZATION |
WOS类目 | Multidisciplinary Sciences |
WOS研究方向 | Science & Technology - Other Topics |
URL | 查看原文 |
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/203227 |
专题 | 资源环境科学 |
作者单位 | 1.Univ Oxford, Div Struct Biol, Wellcome Ctr Human Genet, Oxford OX3 7BN, England; 2.Diamond Light Source Ltd, Harwell Sci & Innovat Campus, Harwell, Berks, England; 3.Fdn Ciencia & Vida, Lab Virol Mol, Ave Zanartu 1482, Santiago 7780272, Chile; 4.Univ Helsinki, Dept Biochem & Dev Biol, Haartmaninkatu 8, FIN-00014 Helsinki, Finland; 5.Thermo Fisher Sci, Achtseweg Noorg 5, NL-5651 GG Eindhoven, Netherlands; 6.Univ Helsinki, Helsinki Inst Life Sci HiLIFE, Inst Biotechnol, Viikinkaari 5, FIN-00014 Helsinki, Finland; 7.Univ Helsinki, Mol & Integrat Biosci Res Program, Viikinkaari 1, FIN-00014 Helsinki, Finland; 8.Univ Helsinki, Helsinki Inst Life Sci HiLIFE, Viikinkaari 1, FIN-00014 Helsinki, Finland; 9.Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China |
推荐引用方式 GB/T 7714 | El Omari, Kamel,Li, Sai,Kotecha, Abhay,et al. The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins[J]. NATURE COMMUNICATIONS,2019,10. |
APA | El Omari, Kamel.,Li, Sai.,Kotecha, Abhay.,Walter, Thomas S..,Bignon, Eduardo A..,...&Roine, Elina.(2019).The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins.NATURE COMMUNICATIONS,10. |
MLA | El Omari, Kamel,et al."The structure of a prokaryotic viral envelope protein expands the landscape of membrane fusion proteins".NATURE COMMUNICATIONS 10(2019). |
条目包含的文件 | 条目无相关文件。 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论