8B59

Rosellinia necatrix megabirnavirus 1-W779 Crown protein

Summary for 8B59

• Entry DOI: 10.2210/pdb8b59/pdb
• EMDB information: 15859
• Descriptor: RnMBV1 Crown protein (1 entity in total)
• Functional Keywords: viruses, dsrna, capsid, cryo-em, fungus, megabirnaviridae, mycoviruses, virus
• Biological source: Rosellinia necatrix megabirnavirus 1/W779
• Total number of polymer chains: 3
• Total formula weight: 455650.50

Authors

Wang, H.,Okamoto, K.,Miyazaki, N.,Suzuki, N. (deposition date: 2022-09-22, release date: 2023-02-22, Last modification date: 2024-07-24)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.3 Å)