CryoEM structure of the tegumented capsid of Epstein-Barr virus.

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.

journal_name

Cell Res

journal_title

Cell research

authors

Li Z,Zhang X,Dong L,Pang J,Xu M,Zhong Q,Zeng MS,Yu X

doi

10.1038/s41422-020-0363-0

subject

Has Abstract

pub_date

2020-10-01 00:00:00

pages

873-884

issue

10

eissn

1001-0602

issn

1748-7838

pii

10.1038/s41422-020-0363-0

journal_volume

30

pub_type

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