7U0D

Local refinement of cryo-EM structure of the interface of the Omicron RBD in complex with antibodies B-182.1 and A19-46.1

7U0D の概要

• エントリーDOI: 10.2210/pdb7u0d/pdb
• 関連するPDBエントリー: 7TCC
• EMDBエントリー: 26256
• 分子名称: Surface glycoprotein, Heavy chain of SARS-CoV-2 antibody A19-46.1, Light chain of SARS-CoV-2 antibody A19-46.1, ... (6 entities in total)
• 機能のキーワード: antibody, sars-cov-2, omicron, b.1.1.529, receptor binding domain, immune system, vral protein-immune system complex, vral 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: 5
• 化学式量合計: 117969.88

構造登録者

Zhou, T.,kwong, P.D. (登録日: 2022-02-17, 公開日: 2022-03-30, 最終更新日: 2025-06-04)

主引用文献

Zhou, T.,Wang, L.,Misasi, J.,Pegu, A.,Zhang, Y.,Harris, D.R.,Olia, A.S.,Talana, C.A.,Yang, E.S.,Chen, M.,Choe, M.,Shi, W.,Teng, I.T.,Creanga, A.,Jenkins, C.,Leung, K.,Liu, T.,Stancofski, E.D.,Stephens, T.,Zhang, B.,Tsybovsky, Y.,Graham, B.S.,Mascola, J.R.,Sullivan, N.J.,Kwong, P.D.
Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.
Science, 376:eabn8897-eabn8897, 2022

PubMed Abstract: The rapid spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.529 (Omicron) variant and its resistance to neutralization by vaccinee and convalescent sera are driving a search for monoclonal antibodies with potent neutralization. To provide insight into effective neutralization, we determined cryo-electron microscopy structures and evaluated receptor binding domain (RBD) antibodies for their ability to bind and neutralize B.1.1.529. Mutations altered 16% of the B.1.1.529 RBD surface, clustered on an RBD ridge overlapping the angiotensin-converting enzyme 2 (ACE2)-binding surface and reduced binding of most antibodies. Substantial inhibitory activity was retained by select monoclonal antibodies-including A23-58.1, B1-182.1, COV2-2196, S2E12, A19-46.1, S309, and LY-CoV1404-that accommodated these changes and neutralized B.1.1.529. We identified combinations of antibodies with synergistic neutralization. The analysis revealed structural mechanisms for maintenance of potent neutralization against emerging variants.

PubMed: 35324257
DOI: 10.1126/science.abn8897

実験手法

ELECTRON MICROSCOPY (4.8 Å)