8ITU

SARS-CoV-2 Omicron BA.1 Spike glycoprotein in complex with rabbit monoclonal antibody 1H1 IgG.

8ITU の概要

• エントリーDOI: 10.2210/pdb8itu/pdb
• EMDBエントリー: 35328
• 分子名称: Spike glycoprotein, 1H1 light chain, 1H1 heavy chain, ... (5 entities in total)
• 機能のキーワード: viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 511130.06

構造登録者

Guo, H.,Gao, Y.,Lu, Y.,Yang, H.,Ji, X. (登録日: 2023-03-23, 公開日: 2023-04-12, 最終更新日: 2024-05-08)

主引用文献

Guo, H.,Yang, Y.,Zhao, T.,Lu, Y.,Gao, Y.,Li, T.,Xiao, H.,Chu, X.,Zheng, L.,Li, W.,Cheng, H.,Huang, H.,Liu, Y.,Lou, Y.,Nguyen, H.C.,Wu, C.,Chen, Y.,Yang, H.,Ji, X.
Mechanism of a rabbit monoclonal antibody broadly neutralizing SARS-CoV-2 variants.
Commun Biol, 6:364-364, 2023

PubMed Abstract: Due to the continuous evolution of SARS-CoV-2, the Omicron variant has emerged and exhibits severe immune evasion. The high number of mutations at key antigenic sites on the spike protein has made a large number of existing antibodies and vaccines ineffective against this variant. Therefore, it is urgent to develop efficient broad-spectrum neutralizing therapeutic drugs. Here we characterize a rabbit monoclonal antibody (RmAb) 1H1 with broad-spectrum neutralizing potency against Omicron sublineages including BA.1, BA.1.1, BA.2, BA.2.12.1, BA.2.75, BA.3 and BA.4/5. Cryo-electron microscopy (cryo-EM) structure determination of the BA.1 spike-1H1 Fab complexes shows that 1H1 targets a highly conserved region of RBD and avoids most of the circulating Omicron mutations, explaining its broad-spectrum neutralization potency. Our findings indicate 1H1 as a promising RmAb model for designing broad-spectrum neutralizing antibodies and shed light on the development of therapeutic agents as well as effective vaccines against newly emerging variants in the future.

PubMed: 37012333
DOI: 10.1038/s42003-023-04759-5

実験手法

ELECTRON MICROSCOPY (3.68 Å)