8HWS

The complex structure of Omicron BA.4 RBD with BD604, S309, and S304

8HWS の概要

• エントリーDOI: 10.2210/pdb8hws/pdb
• EMDBエントリー: 35063
• 分子名称: Spike protein S2', BD-604 Fab Heavy chain, BD-604 Fab Light chain, ... (8 entities in total)
• 機能のキーワード: antibody viral protein complex, immune system/viral protein, immune system-viral protein complex
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 167169.33

構造登録者

He, Q.W.,Xu, Z.P.,Xie, Y.F. (登録日: 2023-01-02, 公開日: 2023-12-06, 最終更新日: 2025-07-16)

主引用文献

He, Q.,Wu, L.,Xu, Z.,Wang, X.,Xie, Y.,Chai, Y.,Zheng, A.,Zhou, J.,Qiao, S.,Huang, M.,Shang, G.,Zhao, X.,Feng, Y.,Qi, J.,Gao, G.F.,Wang, Q.
An updated atlas of antibody evasion by SARS-CoV-2 Omicron sub-variants including BQ.1.1 and XBB.
Cell Rep Med, 4:100991-100991, 2023

PubMed Abstract: Emerging Omicron sub-variants are causing global concerns, and their immune evasion should be monitored continuously. We previously evaluated the escape of Omicron BA.1, BA.1.1, BA.2, and BA.3 from an atlas of 50 monoclonal antibodies (mAbs), covering seven epitope classes of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor-binding domain (RBD). Here, we update the atlas of totally 77 mAbs against emerging sub-variants including BQ.1.1 and XBB and find that BA.4/5, BQ.1.1, and XBB display further evasion. Besides, investigation into the correlation of binding and neutralization of mAbs reveals the important role of antigenic conformation in mAb functioning. Moreover, the complex structures of BA.2 RBD/BD-604/S304 and BA.4/5 RBD/BD-604/S304/S309 further elucidate the molecular mechanism of antibody evasion by these sub-variants. By focusing on the identified broadly potent mAbs, we find a general hotspot epitope on the RBD, which could guide the design of vaccines and calls for new broad-spectrum countermeasures against COVID-19.

PubMed: 37019110
DOI: 10.1016/j.xcrm.2023.100991

実験手法

ELECTRON MICROSCOPY (2.36 Å)