期刊
VIROLOGY
卷 516, 期 -, 页码 239-245出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2018.01.021
关键词
Cryo-electron microscopy; Tomography; Melbournevirus; Marseilleviridae; NCLDV; Virus; Structure; Capsid; Protein complex; Amoeba
类别
资金
- Swedish Research Council [628-20081109, 822-2010-6157, 822-2012-5260, 828-2012-108]
- Knut and Alice Wallenberg Foundation [KAW-2011.081]
- European Research Council [ERC-291602]
- Rontgen-Angstrom Cluster [349-2011-6488, 2015-06107]
- Swedish Foundation for International Cooperation in Research and Higher Education (STINT) [JA2014-5721]
- European Regional Development Fund at the European Extreme Light Infrastructure [ELIBIO CZ.02.1.01/0.0/0.0/15_003/0000447]
- KAKENHI from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan [25251009]
- MEXT of Japan [17H05825]
- Collaborative Study Program of National Institute for Physiological Sciences [38]
- CNRS
- Aix-Marseille University
- French National Research Agency [ANR-14-CE14-0023-01]
- Grants-in-Aid for Scientific Research [16H00786] Funding Source: KAKEN
Nucleocytoplasmic large DNA viruses (NCLDVs) blur the line between viruses and cells. Melbournevirus (MelV, family Marseilleviridae) belongs to a new family of NCLDVs. Here we present an electron cryo-microscopy structure of the MeIV particle, with the large triangulation number T = 309 constructed by 3080 pseudo hexagonal capsomers. The most distinct feature of the particle is a large and dense body (LDB) consistently found inside all particles. Electron cryo-tomography of 147 particles shows that the LDB is preferentially located in proximity to the probable lipid bilayer. The LDB is 30 nm in size and its density matches that of a genome/protein complex. The observed LDB reinforces the structural complexity of MeIV, setting it apart from other NCLDVs.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据
分享论文
