7U2E

Crystal structure of SARS-CoV-2 receptor binding domain in complex with neutralizing antibody ADI-55688

7U2E の概要

• エントリーDOI: 10.2210/pdb7u2e/pdb
• 分子名称: Spike protein S1, ADI-55688 heavy chain, ADI-55688 light chain, ... (5 entities in total)
• 機能のキーワード: sars-cov-2, coronavirus, antibody, spike, rbd, immune system, 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: 3
• 化学式量合計: 71128.75

構造登録者

Yuan, M.,Zhu, X.,Wilson, I.A. (登録日: 2022-02-23, 公開日: 2022-05-04, 最終更新日: 2023-10-25)

主引用文献

Yuan, M.,Zhu, X.,He, W.T.,Zhou, P.,Kaku, C.I.,Capozzola, T.,Zhu, C.Y.,Yu, X.,Liu, H.,Yu, W.,Hua, Y.,Tien, H.,Peng, L.,Song, G.,Cottrell, C.A.,Schief, W.R.,Nemazee, D.,Walker, L.M.,Andrabi, R.,Burton, D.R.,Wilson, I.A.
A broad and potent neutralization epitope in SARS-related coronaviruses.
Proc.Natl.Acad.Sci.USA, 119:e2205784119-e2205784119, 2022

PubMed Abstract: Many neutralizing antibodies (nAbs) elicited to ancestral severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) through natural infection and vaccination have reduced effectiveness to SARS-CoV-2 variants. Here, we show that therapeutic antibody ADG20 is able to neutralize SARS-CoV-2 variants of concern (VOCs) including Omicron (B.1.1.529) as well as other SARS-related coronaviruses. We delineate the structural basis of this relatively escape-resistant epitope that extends from one end of the receptor binding site (RBS) into the highly conserved CR3022 site. ADG20 can then benefit from high potency through direct competition with ACE2 in the more variable RBS and interaction with the more highly conserved CR3022 site. Importantly, antibodies that are able to target this site generally neutralize a broad range of VOCs, albeit with reduced potency against Omicron. Thus, this conserved and vulnerable site can be exploited for the design of universal vaccines and therapeutic antibodies.

PubMed: 35767670
DOI: 10.1073/pnas.2205784119

実験手法

X-RAY DIFFRACTION (2.85 Å)