7WG7

Acidic Omicron Spike Trimer

7WG7 の概要

• エントリーDOI: 10.2210/pdb7wg7/pdb
• EMDBエントリー: 32479
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: sars-cov-2, omicron, spike, acidic, structural 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: 439596.61

構造登録者

Cui, Z. (登録日: 2021-12-28, 公開日: 2022-06-22, 最終更新日: 2025-07-02)

主引用文献

Cui, Z.,Liu, P.,Wang, N.,Wang, L.,Fan, K.,Zhu, Q.,Wang, K.,Chen, R.,Feng, R.,Jia, Z.,Yang, M.,Xu, G.,Zhu, B.,Fu, W.,Chu, T.,Feng, L.,Wang, Y.,Pei, X.,Yang, P.,Xie, X.S.,Cao, L.,Cao, Y.,Wang, X.
Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron.
Cell, 185:860-871.e13, 2022

PubMed Abstract: The SARS-CoV-2 Omicron variant with increased fitness is spreading rapidly worldwide. Analysis of cryo-EM structures of the spike (S) from Omicron reveals amino acid substitutions forging interactions that stably maintain an active conformation for receptor recognition. The relatively more compact domain organization confers improved stability and enhances attachment but compromises the efficiency of the viral fusion step. Alterations in local conformation, charge, and hydrophobic microenvironments underpin the modulation of the epitopes such that they are not recognized by most NTD- and RBD-antibodies, facilitating viral immune escape. Structure of the Omicron S bound with human ACE2, together with the analysis of sequence conservation in ACE2 binding region of 25 sarbecovirus members, as well as heatmaps of the immunogenic sites and their corresponding mutational frequencies, sheds light on conserved and structurally restrained regions that can be used for the development of broad-spectrum vaccines and therapeutics.

PubMed: 35120603
DOI: 10.1016/j.cell.2022.01.019

実験手法

ELECTRON MICROSCOPY (4 Å)