9L2L

Structure of SARS-CoV-2 EG.5.1 Variant Spike protein complexed with antibody XGi-198

9L2L の概要

• エントリーDOI: 10.2210/pdb9l2l/pdb
• 関連するPDBエントリー: 9L05
• EMDBエントリー: 62777
• 分子名称: Spike glycoprotein, XGi-198 heavy chain, XGi-198 light chain, ... (6 entities in total)
• 機能のキーワード: spike-antibody complex, viral protein/immune system, viral protein-immune system complex
• 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: 18
• 化学式量合計: 1323516.81

構造登録者

Qiu, Y.N.,Sun, L. (登録日: 2024-12-17, 公開日: 2025-12-10)

主引用文献

Xie, M.,Qiu, Y.,Zhao, X.,Shi, J.,Liu, Y.,Zhang, Q.,He, J.,Li, J.,Liu, L.,Sun, S.,Zhu, Y.,Mao, Q.,Long, Y.,Oliveira, T.Y.,Wang, Z.,Zhou, Y.,Yan, Y.,Xia, A.,Zai, W.,Mayer, C.T.,Xie, Y.,Jiang, S.,Lu, L.,Xia, R.,Wu, F.,Sun, L.,Wang, P.,Chu, H.,Wang, Q.
Orphan broadly RBD-binding antibodies annotate three remaining conserved RBD epitopes along SARS-CoV-2 evolution.
Nat Commun, 16:10566-10566, 2025

PubMed Abstract: The receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein continues to evolve, facilitating antibody evasion. It remains unclear whether any conserved RBD epitopes persist across SARS-CoV-2 variants and whether vaccination and/or breakthrough infection (BTI) can elicit antibodies capable of targeting these conserved regions to counter future variants. Here, using a heterogeneous double-bait single B-cell sorting strategy, we identify a subset of antibodies with broad-spectrum RBD binding, including recognition of SARS-CoV-1 and emerging variants such as EG.5.1, BA.2.86, JN.1, and KP.2/3. These broadly binding antibodies (bbAbs) exhibit elevated levels of somatic hypermutation but are infrequently derived from clonally expanded B lymphocytes. Passive transfer of representative bbAbs reduces viral infection in a male hamster model. Structural analyses reveals that these bbAbs primarily target three distinct, highly conserved RBD epitopes, suggesting potential regions of future mutational pressure and highlighting the presence of conserved and immunogenic RBD conformations that may serve as a foundation for the development of broadly protective vaccines.

PubMed: 41298374
DOI: 10.1038/s41467-025-65596-0

実験手法

ELECTRON MICROSCOPY (2.98 Å)