7XR3

3.4 Angstrom cryoEM D5 reconstruction of mud crab reovirus

Summary for 7XR3

• Entry DOI: 10.2210/pdb7xr3/pdb
• EMDB information: 33404
• Descriptor: VP3, VP1 (2 entities in total)
• Functional Keywords: reovirus, ds-rna virus, virus
• Biological source: Scylla serrata reovirus SZ-2007; More
• Total number of polymer chains: 11
• Total formula weight: 1131682.36

Authors

Zhang, Q.F.,Gao, Y.Z. (deposition date: 2022-05-09, release date: 2023-04-19, Last modification date: 2024-07-03)

Primary citation

Zhang, Q.,Gao, Y.,Baker, M.L.,Liu, S.,Jia, X.,Xu, H.,He, J.,Kaelber, J.T.,Weng, S.,Jiang, W.
The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.
Plos Pathog., 19:e1011341-e1011341, 2023

PubMed Abstract: Infecting a wide range of hosts, members of Reovirales (formerly Reoviridae) consist of a genome with different numbers of segmented double stranded RNAs (dsRNA) encapsulated by a proteinaceous shell and carry out genome replication and transcription inside the virion. Several cryo-electron microscopy (cryo-EM) structures of reoviruses with 9, 10 or 11 segmented dsRNA genomes have revealed insights into genome arrangement and transcription. However, the structure and genome arrangement of 12-segmented Reovirales members remain poorly understood. Using cryo-EM, we determined the structure of mud crab reovirus (MCRV), a 12-segmented dsRNA virus that is a putative member of Reovirales in the non-turreted Sedoreoviridae family, to near-atomic resolutions with icosahedral symmetry (3.1 Å) and without imposing icosahedral symmetry (3.4 Å). These structures revealed the organization of the major capsid proteins in two layers: an outer T = 13 layer consisting of VP12 trimers and unique VP11 clamps, and an inner T = 1 layer consisting of VP3 dimers. Additionally, ten RNA dependent RNA polymerases (RdRp) were well resolved just below the VP3 layer but were offset from the 5-fold axes and arranged with D5 symmetry, which has not previously been seen in other members of Reovirales. The N-termini of VP3 were shown to adopt four unique conformations; two of which anchor the RdRps, while the other two conformations are likely involved in genome organization and capsid stability. Taken together, these structures provide a new level of understanding for capsid stabilization and genome organization of segmented dsRNA viruses.

PubMed: 37083840
DOI: 10.1371/journal.ppat.1011341

Experimental method

ELECTRON MICROSCOPY (3.7 Å)