7E8M

Crystal structure of SARS-CoV-2 antibody P2C-1F11 with mutated RBD

7E8M の概要

• エントリーDOI: 10.2210/pdb7e8m/pdb
• 分子名称: Spike protein S1, antibody P2C-1F11 heavy chain, antibody P2C-1F11 light chain, ... (5 entities in total)
• 機能のキーワード: sars-cov-2 spike, receptor binding domain, antibody, viral protein, viral protein-immune system complex, viral protein/immune system
• 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: 3
• 化学式量合計: 68255.12

構造登録者

Wang, X.Q.,Zhang, L.Q.,Ge, J.W.,Wang, R.K.,Lan, J. (登録日: 2021-03-02, 公開日: 2021-05-26, 最終更新日: 2024-11-20)

主引用文献

Wang, R.,Zhang, Q.,Ge, J.,Ren, W.,Zhang, R.,Lan, J.,Ju, B.,Su, B.,Yu, F.,Chen, P.,Liao, H.,Feng, Y.,Li, X.,Shi, X.,Zhang, Z.,Zhang, F.,Ding, Q.,Zhang, T.,Wang, X.,Zhang, L.
Analysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability to use ACE2 receptors from additional species.
Immunity, 54:1611-1621.e5, 2021

PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants continue to emerge during the global pandemic and may facilitate escape from current antibody therapies and vaccine protection. Here we showed that the South African variant B.1.351 was the most resistant to current monoclonal antibodies and convalescent plasma from coronavirus disease 2019 (COVID-19)-infected individuals, followed by the Brazilian variant P.1 and the United Kingdom variant B.1.1.7. This resistance hierarchy corresponded with Y144del and 242-244del mutations in the N-terminal domain and K417N/T, E484K, and N501Y mutations in the receptor-binding domain (RBD) of SARS-CoV-2. Crystal structure analysis of the B.1.351 triple mutant (417N-484K-501Y) RBD complexed with the monoclonal antibody P2C-1F11 revealed the molecular basis for antibody neutralization and escape. B.1.351 and P.1 also acquired the ability to use mouse and mink ACE2 receptors for entry. Our results demonstrate major antigenic shifts and potential broadening of the host range for B.1.351 and P.1 variants, which poses serious challenges to current antibody therapies and vaccine protection.

PubMed: 34166623
DOI: 10.1016/j.immuni.2021.06.003

実験手法

X-RAY DIFFRACTION (2.09 Å)