8B4Z

Rosellinia necatrix megabirnavirus 1-W779 full capsid

8B4Z の概要

• エントリーDOI: 10.2210/pdb8b4z/pdb
• EMDBエントリー: 15855
• 分子名称: Major capsid protein A (1 entity in total)
• 機能のキーワード: viruses, dsrna, capsid, cryo-em, fungus, megabirnaviridae, mycoviruses, virus
• 由来する生物種: Rosellinia necatrix megabirnavirus 1/W779
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 272169.91

構造登録者

Wang, H.,Okamoto, K.,Miyazaki, N.,Suzuki, N. (登録日: 2022-09-21, 公開日: 2023-02-22, 最終更新日: 2024-07-24)

主引用文献

Wang, H.,Salaipeth, L.,Miyazaki, N.,Suzuki, N.,Okamoto, K.
Capsid structure of a fungal dsRNA megabirnavirus reveals its previously unidentified surface architecture.
Plos Pathog., 19:e1011162-e1011162, 2023

PubMed Abstract: Rosellinia necatrix megabirnavirus 1-W779 (RnMBV1) is a non-enveloped icosahedral double-stranded (ds)RNA virus that infects the ascomycete fungus Rosellinia necatrix, a causative agent that induces a lethal plant disease white root rot. Herein, we have first resolved the atomic structure of the RnMBV1 capsid at 3.2 Å resolution using cryo-electron microscopy (cryo-EM) single-particle analysis. Compared with other non-enveloped icosahedral dsRNA viruses, the RnMBV1 capsid protein structure exhibits an extra-long C-terminal arm and a surface protrusion domain. In addition, the previously unrecognized crown proteins are identified in a symmetry-expanded cryo-EM model and are present over the 3-fold axes. These exclusive structural features of the RnMBV1 capsid could have been acquired for playing essential roles in transmission and/or particle assembly of the megabirnaviruses. Our findings, therefore, will reinforce the understanding of how the structural and molecular machineries of the megabirnaviruses influence the virulence of the disease-related ascomycete fungus.

PubMed: 36848381
DOI: 10.1371/journal.ppat.1011162

実験手法

ELECTRON MICROSCOPY (3.2 Å)