7BSI

Epstein-Barr virus, one asymmetric unit structure of the icosahedral tegumented capsid

This is a non-PDB format compatible entry.

Summary for 7BSI

• Entry DOI: 10.2210/pdb7bsi/pdb
• EMDB information: 30162
• Descriptor: Small capsomere-interacting protein, Major capsid protein, Triplex capsid protein 1, ... (4 entities in total)
• Functional Keywords: tegumented capsid, icosahedral reconstruction, virus
• Biological source: Epstein-Barr virus (strain B95-8) (HHV-4); More
• Total number of polymer chains: 47
• Total formula weight: 3288792.93

Authors

Li, Z.,Yu, X. (deposition date: 2020-03-30, release date: 2020-09-30, Last modification date: 2024-10-16)

Primary citation

Li, Z.,Zhang, X.,Dong, L.,Pang, J.,Xu, M.,Zhong, Q.,Zeng, M.S.,Yu, X.
CryoEM structure of the tegumented capsid of Epstein-Barr virus.
Cell Res., 30:873-884, 2020

PubMed Abstract: Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection.

PubMed: 32620850
DOI: 10.1038/s41422-020-0363-0

Experimental method

ELECTRON MICROSCOPY (4.1 Å)