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TitleMegabirnavirus structure reveals a putative 120-subunit capsid formed by asymmetrical dimers with distinctive large protrusions.
Journal, issue, pagesJ Gen Virol, Vol. 96, Issue 8, Page 2435-2441, Year 2015
Publish dateMay 12, 2015
AuthorsNaoyuki Miyazaki / Lakha Salaipeth / Satoko Kanematsu / Kenji Iwasaki / Nobuhiro Suzuki /
PubMed AbstractRosellinia necatrix megabirnavirus 1 (RnMBV1) W779 is a bi-segmented dsRNA virus and a strain of the type species Rosellinia necatrix megabirnavirus 1 of the family Megabirnaviridae. RnMBV1 causes ...Rosellinia necatrix megabirnavirus 1 (RnMBV1) W779 is a bi-segmented dsRNA virus and a strain of the type species Rosellinia necatrix megabirnavirus 1 of the family Megabirnaviridae. RnMBV1 causes severe reduction of both mycelial growth of Rosellinia necatrix in synthetic medium and fungal virulence to plant hosts, and thus has strong potential for virocontrol (biological control using viruses) of white rot. The structure of RnMBV1 was examined by cryo-electron microscopy and three-dimensional reconstruction at 15.7 Å resolution. The diameter of the RnMBV1 capsid was 520 Å, and the capsid was composed of 60 asymmetrical dimers in the T = 1 (so-called T = 2) lattice that is well conserved among dsRNA viruses. However, RnMBV1 has putatively 120 large protrusions with a width of ∼ 45 Å and a height of ∼ 50 Å on the virus surface, making it distinguishable from the other dsRNA viruses.
External linksJ Gen Virol / PubMed:25968130
MethodsEM (single particle)
Resolution11.6 - 14.9 Å
Structure data

EMDB-2931:
CryoEM single particle reconstruction of a full particle of Rosellinia necatrix megabirnavirus
Method: EM (single particle) / Resolution: 13.0 Å

EMDB-2932:
Cryo-EM single particle reconstruction of an empty particle of Rosellinia necatrix megabirnavirus 1
Method: EM (single particle) / Resolution: 14.9 Å

EMDB-2933:
Cryo-EM single particle reconstruction of Rosellinia necatrix megabirnavirus 1 reconstructed with the mixture of empty and full particles
Method: EM (single particle) / Resolution: 11.6 Å

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