7Y71

SARS-CoV-2 spike glycoprotein trimer complexed with Fab fragment of anti-RBD antibody E7

7Y71 の概要

• エントリーDOI: 10.2210/pdb7y71/pdb
• EMDBエントリー: 33650
• 分子名称: Fab E7 light chain, Fab E7 heavy chain, Spike glycoprotein, ... (5 entities in total)
• 機能のキーワード: viral protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 451908.01

構造登録者

Chia, W.N.,Tan, C.W.,Tan, A.W.K.,Young, B.,Starr, T.N.,Lopez, E.,Fibriansah, G.,Barr, J.,Cheng, S.,Yeoh, A.Y.Y.,Yap, W.C.,Lim, B.L.,Ng, T.S.,Sia, W.R.,Zhu, F.,Chen, S.,Zhang, J.,Greaney, A.J.,Chen, M.,Au, G.G.,Paradkar, P.,Peiris, M.,Chung, A.W.,Bloom, J.D.,Lye, D.,Lok, S.M.,Wang, L.F. (登録日: 2022-06-21, 公開日: 2023-08-02, 最終更新日: 2024-10-23)

主引用文献

Chia, W.N.,Tan, C.W.,Tan, A.W.K.,Young, B.,Starr, T.N.,Lopez, E.,Fibriansah, G.,Barr, J.,Cheng, S.,Yeoh, A.Y.,Yap, W.C.,Lim, B.L.,Ng, T.S.,Sia, W.R.,Zhu, F.,Chen, S.,Zhang, J.,Kwek, M.S.S.,Greaney, A.J.,Chen, M.,Au, G.G.,Paradkar, P.N.,Peiris, M.,Chung, A.W.,Bloom, J.D.,Lye, D.,Lok, S.,Wang, L.F.
Potent pan huACE2-dependent sarbecovirus neutralizing monoclonal antibodies isolated from a BNT162b2-vaccinated SARS survivor.
Sci Adv, 9:eade3470-eade3470, 2023

PubMed Abstract: The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern such as Omicron hampered efforts in controlling the ongoing coronavirus disease 2019 pandemic due to their ability to escape neutralizing antibodies induced by vaccination or prior infection, highlighting the need to develop broad-spectrum vaccines and therapeutics. Most human monoclonal antibodies (mAbs) reported to date have not demonstrated true pan-sarbecovirus neutralizing breadth especially against animal sarbecoviruses. Here, we report the isolation and characterization of highly potent mAbs targeting the receptor binding domain (RBD) of huACE2-dependent sarbecovirus from a SARS-CoV survivor vaccinated with BNT162b2. Among the six mAbs identified, one (E7) showed better huACE2-dependent sarbecovirus neutralizing potency and breadth than any other mAbs reported to date. Mutagenesis and cryo-electron microscopy studies indicate that these mAbs have a unique RBD contact footprint and that E7 binds to a quaternary structure-dependent epitope.

PubMed: 37494438
DOI: 10.1126/sciadv.ade3470

実験手法

ELECTRON MICROSCOPY (3.12 Å)