7XS8

Crystal structure of SARS-CoV-2 spike receptor binding domain bound with P5S-1H1 Fab

7XS8 の概要

• エントリーDOI: 10.2210/pdb7xs8/pdb
• 分子名称: P5S-1H1 Heavy chain, Spike protein S1, P5S-1H1 Light chain, ... (4 entities in total)
• 機能のキーワード: sars-cov-2, antibody, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 67844.82

構造登録者

Wang, X.,Wang, Z. (登録日: 2022-05-13, 公開日: 2023-04-26, 最終更新日: 2024-10-16)

主引用文献

Ju, B.,Zhang, Q.,Wang, Z.,Aw, Z.Q.,Chen, P.,Zhou, B.,Wang, R.,Ge, X.,Lv, Q.,Cheng, L.,Zhang, R.,Wong, Y.H.,Chen, H.,Wang, H.,Shan, S.,Liao, X.,Shi, X.,Liu, L.,Chu, J.J.H.,Wang, X.,Zhang, Z.,Zhang, L.
Infection with wild-type SARS-CoV-2 elicits broadly neutralizing and protective antibodies against omicron subvariants.
Nat.Immunol., 24:690-699, 2023

PubMed Abstract: The omicron variants of SARS-CoV-2 have substantial ability to escape infection- and vaccine-elicited antibody immunity. Here, we investigated the extent of such escape in nine convalescent patients infected with the wild-type SARS-CoV-2 during the first wave of the pandemic. Among the total of 476 monoclonal antibodies (mAbs) isolated from peripheral memory B cells, we identified seven mAbs with broad neutralizing activity to all variants tested, including various omicron subvariants. Biochemical and structural analysis indicated the majority of these mAbs bound to the receptor-binding domain, mimicked the receptor ACE2 and were able to accommodate or inadvertently improve recognition of omicron substitutions. Passive delivery of representative antibodies protected K18-hACE2 mice from infection with omicron and beta SARS-CoV-2. A deeper understanding of how the memory B cells that produce these antibodies could be selectively boosted or recalled can augment antibody immunity against SARS-CoV-2 variants.

PubMed: 36914890
DOI: 10.1038/s41590-023-01449-6

実験手法

X-RAY DIFFRACTION (2.8 Å)