8XY9

Crystal structure of SARS-CoV-2 BF.7 RBD and human ACE2 complex

8XY9 の概要

• エントリーDOI: 10.2210/pdb8xy9/pdb
• 分子名称: Processed angiotensin-converting enzyme 2, Spike protein S1, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: sars-cov-2 bf.7, ace2, viral protein/hydrolase, viral protein-hydrolase complex
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 186781.97

構造登録者

Lan, J.,Wang, C.H. (登録日: 2024-01-19, 公開日: 2025-01-22, 最終更新日: 2025-04-16)

主引用文献

Wang, C.,Zhang, Y.,Yang, C.,Ren, W.,Qiu, C.,Fan, S.,Ding, Q.,Lan, J.
Receptor binding mechanism and immune evasion capacity of SARS-CoV-2 BQ.1.1 lineage.
Virology, 600:110241-110241, 2024

PubMed Abstract: The global spread of COVID-19 remains a significant threat to human health. The SARS-CoV-2 BQ.1.1 lineage, including BA.5.2, BF.7, BQ.1 and BQ.1.1, caused a new soaring of infection cases due to rapid transmission. However, the receptor binding mechanism and immune evasion capacity of these variants need to be explored further. Our study found that while the BA.5.2, BF.7 and BQ.1.1 variants pseudovirus had similar cell entry efficiency, the BF.7 and BQ.1.1 RBD bound to human ACE2 (hACE2) with a slightly stronger affinity than the BA.5.2 RBD. Structural analysis revealed R346T, K444T, and N460K mutations altered RBD-hACE2 binding interface details and surface electrostatic potential of BQ.1.1 RBD. Serum neutralization tests showed BQ.1.1 variant had stronger immune evasion capacity than BA.5.2 and BF.7 variants. Our findings illustrated the receptor binding mechanism and serological neutralization activity of the BA.5.2, BF.7 and BQ.1.1 variants, which verified the necessity for further antibody therapy optimization and vaccination development.

PubMed: 39270455
DOI: 10.1016/j.virol.2024.110241

実験手法

X-RAY DIFFRACTION (3.64 Å)