7Y6D

Cryo-EM structure of SARS-CoV-2 Delta variant spike proteins on intact virions: 3 Closed RBD

7Y6D の概要

• エントリーDOI: 10.2210/pdb7y6d/pdb
• EMDBエントリー: 33205
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: trimer, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV,SARS-CoV-2)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 438120.04

構造登録者

Xu, J.,Song, Y.,Li, S. (登録日: 2022-06-20, 公開日: 2023-06-07, 最終更新日: 2024-11-06)

主引用文献

Song, Y.,Yao, H.,Wu, N.,Xu, J.,Zhang, Z.,Peng, C.,Li, S.,Kong, W.,Chen, Y.,Zhu, M.,Wang, J.,Shi, D.,Zhao, C.,Lu, X.,Echavarria Galindo, M.,Li, S.
In situ architecture and membrane fusion of SARS-CoV-2 Delta variant.
Proc.Natl.Acad.Sci.USA, 120:e2213332120-e2213332120, 2023

PubMed Abstract: Among the current five Variants of Concern, infections caused by SARS-CoV-2 B.1.617.2 (Delta) variant are often associated with the greatest severity. Despite recent advances on the molecular basis of elevated pathogenicity using recombinant proteins, the architecture of intact Delta virions remains veiled. Moreover, pieces of molecular evidence for the detailed mechanism of S-mediated membrane fusion are missing. Here, we showed the pleomorphic nature of Delta virions from electron beam inactivated samples and reported the in situ structure and distribution of S on the authentic Delta variant. We also captured the virus-virus fusion events, which provided pieces of structural evidence for Delta's attenuated dependency on cellular factors for fusion activation, and proposed a model of S-mediated membrane fusion. Besides, site-specific glycan analysis revealed increased oligomannose-type glycosylation of native Delta S than that of the WT S. Together, these results disclose distinctive factors of Delta being the most virulent SARS-CoV-2 variant.

PubMed: 37094167
DOI: 10.1073/pnas.2213332120

実験手法

ELECTRON MICROSCOPY (4.39 Å)