8B3J

Chaetoceros socialis forma radians RNA virus 1 empty capsid atomic model

Summary for 8B3J

• Entry DOI: 10.2210/pdb8b3j/pdb
• EMDB information: 15830
• Descriptor: Structural polyprotein (3 entities in total)
• Functional Keywords: icosahedral, empty particle capsid, virus
• Biological source: Chaetoceros socialis forma radians RNA virus 1; More
• Total number of polymer chains: 3
• Total formula weight: 87900.58

Authors

Wang, H.,Okamoto, K.,Munke, A. (deposition date: 2022-09-16, release date: 2022-11-23, Last modification date: 2024-07-24)

Primary citation

Wang, H.,Munke, A.,Li, S.,Tomaru, Y.,Okamoto, K.
Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses.
Viruses, 14:-, 2022

PubMed Abstract: viruses are abundant algal viruses that regulate the dynamics of algal blooms in aquatic environments. They employ a narrow host range because they merely lyse their algal host species. This host-specific lysis is thought to correspond to the unique receptor-binding mechanism of the viruses. Here, we present the atomic structures of the full and empty capsids of Chaetoceros socialis forma radians RNA virus 1 built-in 3.0 Å and 3.1 Å cryo-electron microscopy maps. The empty capsid structure and the structural variability provide insights into its assembly and uncoating intermediates. In conjunction with the previously reported atomic model of the Chaetoceros tenuissimus RNA virus type II capsid, we have identified the common and diverse structural features of the VP1 surface between the viruses. We have also tested the potential usage of AlphaFold2 for structural prediction of the VP1s and a subsequent structural phylogeny for classifying viruses by their hosts. These findings will be crucial for inferring the host-specific receptor-binding mechanism in viruses.

PubMed: 36366467
DOI: 10.3390/v14112369

Experimental method

ELECTRON MICROSCOPY (3.1 Å)