Virus: Human gammaherpesvirus 4 (Epstein-Barr virus)
Function / homology
Function and homology information
T=16 icosahedral viral capsid / viral capsid assembly / viral process / viral capsid / host cell nucleus / structural molecule activity / DNA binding Similarity search - Function
Gammaherpesvirus capsid / Gammaherpesvirus capsid protein / Herpesvirus capsid shell protein 1 / Herpesvirus capsid shell protein VP19C / Herpesvirus capsid protein 2 / Herpesvirus VP23 like capsid protein / Herpesvirus major capsid protein / Herpesvirus major capsid protein, upper domain superfamily / Herpes virus major capsid protein Similarity search - Domain/homology
Triplex capsid protein 1 / Major capsid protein / Small capsomere-interacting protein / Triplex capsid protein 2 Similarity search - Component
Biological species
Human gammaherpesvirus 4 (Epstein-Barr virus)
Method
single particle reconstruction / cryo EM / Resolution: 3.5 Å
National Natural Science Foundation of China (NSFC)
31900869
China
National Natural Science Foundation of China (NSFC)
81702001
China
National Natural Science Foundation of China (NSFC)
81830090
China
Ministry of Science and Technology (MoST, China)
2016YFA0502101
China
Ministry of Science and Technology (MoST, China)
2017YFA0505600
China
Citation
Journal: Cell Res / Year: 2020 Title: CryoEM structure of the tegumented capsid of Epstein-Barr virus. Authors: Zhihai Li / Xiao Zhang / Lili Dong / Jingjing Pang / Miao Xu / Qian Zhong / Mu-Sheng Zeng / Xuekui Yu / 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, ...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.
History
Deposition
Mar 23, 2020
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Header (metadata) release
Sep 30, 2020
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Map release
Sep 30, 2020
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Update
Oct 14, 2020
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Current status
Oct 14, 2020
Processing site: PDBj / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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