7THK

Cryo-EM structure of prefusion SARS-CoV-2 spike omicron B.1.1.529 variant

7THK の概要

• エントリーDOI: 10.2210/pdb7thk/pdb
• EMDBエントリー: 25896
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: fusion protein, spike glycoprotein, covid-19, rbd, ntd, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 426815.81

構造登録者

Cerutti, G.,Shapiro, L. (登録日: 2022-01-11, 公開日: 2022-03-02, 最終更新日: 2024-11-06)

主引用文献

Cerutti, G.,Guo, Y.,Liu, L.,Liu, L.,Zhang, Z.,Luo, Y.,Huang, Y.,Wang, H.H.,Ho, D.D.,Sheng, Z.,Shapiro, L.
Cryo-EM structure of the SARS-CoV-2 Omicron spike.
Cell Rep, 38:110428-110428, 2022

PubMed Abstract: The recently reported B.1.1.529 Omicron variant of severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) includes 34 mutations in the spike protein relative to the Wuhan strain, including 15 mutations in the receptor-binding domain (RBD). Functional studies have shown Omicron to substantially escape the activity of many SARS-CoV-2-neutralizing antibodies. Here, we report a 3.1 Å-resolution cryoelectron microscopy (cryo-EM) structure of the Omicron spike protein ectodomain. The structure depicts a spike that is exclusively in the 1-RBD-up conformation with high mobility of RBD. Many mutations cause steric clashes and/or altered interactions at antibody-binding surfaces, whereas others mediate changes of the spike structure in local regions to interfere with antibody recognition. Overall, the structure of the Omicron spike reveals how mutations alter its conformation and explains its extraordinary ability to evade neutralizing antibodies.

PubMed: 35172173
DOI: 10.1016/j.celrep.2022.110428

実験手法

ELECTRON MICROSCOPY (3.11 Å)