7X2A

MERS-CoV spike complex with S41 neutralizing antibody Fab Class1 (1u2d RBD with 1Fab)

7X2A の概要

• エントリーDOI: 10.2210/pdb7x2a/pdb
• EMDBエントリー: 32963
• 分子名称: MERS-CoV Spike glycoprotein, antibody S41 heavy chain, antibody S41 light chain (3 entities in total)
• 機能のキーワード: receptor binding domain, viral protein
• 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: 492057.43

構造登録者

Zeng, J.W.,Zhang, S.Y.,Zhou, H.X.,Wang, X.W. (登録日: 2022-02-25, 公開日: 2022-11-09, 最終更新日: 2024-10-23)

主引用文献

Zhang, S.,Jia, W.,Zeng, J.,Li, M.,Wang, Z.,Zhou, H.,Zhang, L.,Wang, X.
Cryoelectron microscopy structures of a human neutralizing antibody bound to MERS-CoV spike glycoprotein.
Front Microbiol, 13:988298-988298, 2022

PubMed Abstract: Neutralizing monoclonal antibodies (mAbs) against highly pathogenic coronaviruses represent promising candidates for clinical intervention. Here, we isolated a potent neutralizing monoclonal antibody, MERS-S41, from a yeast displayed scFv library using the S protein as a bait. To uncover the neutralization mechanism, we determined structures of MERS-S41 Fab in complex with the trimeric spike glycoprotein by cryoelectron microscopy (cryo-EM). We observed four distinct classes of the complex structure, which showed that the MERS-S41 Fab bound to the "up" receptor binding domain (RBD) with full saturation and also bound to an accessible partially lifted "down" RBD, providing a structural basis for understanding how mAbs bind to trimeric spike glycoproteins. Structure analysis of the epitope and cell surface staining assays demonstrated that virus entry is blocked predominantly by direct competition with the host receptor, dipeptidyl peptidase-4 (DPP4).

PubMed: 36246239
DOI: 10.3389/fmicb.2022.988298

実験手法

ELECTRON MICROSCOPY (2.49 Å)