8GNH
Complex structure of BD-218 and Spike protein
8GNH の概要
| エントリーDOI | 10.2210/pdb8gnh/pdb |
| EMDBエントリー | 34164 |
| 分子名称 | Spike glycoprotein, Heavy chain of BD-218, Light chain of BD-218, ... (5 entities in total) |
| 機能のキーワード | sars-cov-2, neutralizing monoclonal antibody, antiviral protein, viral protein-antiviral protein complex, viral protein/antiviral 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 | 469326.87 |
| 構造登録者 | |
| 主引用文献 | Wang, B.,Xu, H.,Liang, Z.T.,Zhao, T.N.,Zhang, X.,Peng, T.B.,Wang, Y.C.,Su, X.D. Human antibody BD-218 has broad neutralizing activity against concerning variants of SARS-CoV-2. Int.J.Biol.Macromol., 227:896-902, 2023 Cited by PubMed Abstract: As SARS-CoV-2 variants of concern (VOC) reduce the effectiveness of existing anti-COVID therapeutics, it is increasingly critical to identify highly potent neutralizing antibodies (nAbs) that bind to conserved regions across multiple variants, especially beta, delta, and omicron variants. Using single-cell sequencing with biochemical methods and pseudo-typed virus neutralization experiments, here we report the characterization of a potent nAb BD-218, identified from an early screen of patients recovering from the original virus. We have determined the cryo-EM structure of the BD-218/spike protein complex to define its epitope in detail, which revealed that BD-218 interacts with a novel epitope on the receptor-binding domain (RBD) of the spike protein. We concluded that BD-218 is a highly effective and broadly active nAb against SARS-CoV-2 variants with promising potential for therapeutic development. PubMed: 36528147DOI: 10.1016/j.ijbiomac.2022.12.120 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.74 Å) |
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