6W2D

Structures of Capsid and Capsid-Associated Tegument Complex inside the Epstein-Barr Virus

6W2D の概要

• エントリーDOI: 10.2210/pdb6w2d/pdb
• EMDBエントリー: 21504 21505 21506 21507 21508 21510 21515 21525 21526 21527
• 分子名称: Major capsid protein, Capsid vertex component 1, Capsid vertex component 2, ... (7 entities in total)
• 機能のキーワード: gamma-herpesvirus, ebv, catc, structural plasticity, viral protein
• 由来する生物種: Epstein-Barr virus (strain B95-8) (HHV-4); 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 1930559.00

構造登録者

Liu, W.,Cui, Y.X.,Wang, C.Y.,Li, Z.H.,Gong, D.Y.,Dai, X.H.,Bi, G.Q.,Sun, R.,Zhou, Z.H. (登録日: 2020-03-05, 公開日: 2020-07-15, 最終更新日: 2024-03-06)

主引用文献

Liu, W.,Cui, Y.,Wang, C.,Li, Z.,Gong, D.,Dai, X.,Bi, G.Q.,Sun, R.,Zhou, Z.H.
Structures of capsid and capsid-associated tegument complex inside the Epstein-Barr virus.
Nat Microbiol, 5:1285-1298, 2020

PubMed Abstract: As the first discovered human cancer virus, Epstein-Barr virus (EBV) causes Burkitt's lymphoma and nasopharyngeal carcinoma. Isolating virions for determining high-resolution structures has been hindered by latency-a hallmark of EBV infection-and atomic structures are thus available only for recombinantly expressed EBV proteins. In the present study, by symmetry relaxation and subparticle reconstruction, we have determined near-atomic-resolution structures of the EBV capsid with an asymmetrically attached DNA-translocating portal and capsid-associated tegument complexes from cryogenic electron microscopy images of just 2,048 EBV virions obtained by chemical induction. The resulting atomic models reveal structural plasticity among the 20 conformers of the major capsid protein, 2 conformers of the small capsid protein (SCP), 4 conformers of the triplex monomer proteins and 2 conformers of the triplex dimer proteins. Plasticity reaches the greatest level at the capsid-tegument interfaces involving SCP and capsid-associated tegument complexes (CATC): SCPs crown pentons/hexons and mediate tegument protein binding, and CATCs bind and rotate all five periportal triplexes, but notably only about one peri-penton triplex. These results offer insights into the EBV capsid assembly and a mechanism for recruiting cell-regulating factors into the tegument compartment as 'cargoes', and should inform future anti-EBV strategies.

PubMed: 32719506
DOI: 10.1038/s41564-020-0758-1

実験手法

ELECTRON MICROSCOPY (4 Å)