| Literature DB >> 29407382 |
Kenta Okamoto1, Naoyuki Miyazaki2, Hemanth K N Reddy3, Max F Hantke3, Filipe R N C Maia3, Daniel S D Larsson3, Chantal Abergel4, Jean-Michel Claverie5, Janos Hajdu6, Kazuyoshi Murata7, Martin Svenda3.
Abstract
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 MelV 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 MelV, setting it apart from other NCLDVs.Entities:
Keywords: Amoeba; Capsid; Cryo-electron microscopy; Marseilleviridae; Melbournevirus; NCLDV; Protein complex; Structure; Tomography; Virus
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Year: 2018 PMID： 29407382 DOI： 10.1016/j.virol.2018.01.021
Source DB: PubMed Journal: Virology ISSN： 0042-6822 Impact factor: 3.616