Cryo-EM structure of a Marseilleviridae virus particle reveals a large internal microassembly
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
29407382
DOI
10.1016/j.virol.2018.01.021
PII: S0042-6822(18)30028-X
Knihovny.cz E-resources
- Keywords
- Amoeba, Capsid, Cryo-electron microscopy, Marseilleviridae, Melbournevirus, NCLDV, Protein complex, Structure, Tomography, Virus,
- MeSH
- DNA Viruses genetics physiology ultrastructure MeSH
- Cryoelectron Microscopy MeSH
- Genome, Viral MeSH
- Capsid metabolism ultrastructure MeSH
- Virus Assembly MeSH
- Virion genetics physiology ultrastructure MeSH
- Viral Proteins genetics metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Viral Proteins MeSH
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.
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