7BR7

Epstein-Barr virus, C1 portal-proximal penton vertex, CATC binding

Summary for 7BR7

• Entry DOI: 10.2210/pdb7br7/pdb
• EMDB information: 30158
• Descriptor: Capsid vertex component 2, Capsid vertex component 1, Large tegument protein deneddylase, ... (7 entities in total)
• Functional Keywords: portal-proximal penton vertex, catc binding, tegumented capsid, asymmetric reconstruction, viral protein
• Biological source: Epstein-Barr virus (strain B95-8) (HHV-4); More
• Total number of polymer chains: 21
• Total formula weight: 1930559.00

Authors

Li, Z.,Yu, X. (deposition date: 2020-03-26, release date: 2020-09-30, Last modification date: 2025-06-25)

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 (4.3 Å)