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-Structure paper
タイトル | Human antibody BD-218 has broad neutralizing activity against concerning variants of SARS-CoV-2. |
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ジャーナル・号・ページ | Int J Biol Macromol, Vol. 227, Page 896-902, Year 2023 |
掲載日 | 2023年2月1日 |
著者 | Bo Wang / Hua Xu / Zi-Teng Liang / Tian-Ning Zhao / Xin Zhang / Tian-Bo Peng / You-Chun Wang / Xiao-Dong Su / |
PubMed 要旨 | 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 ...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. |
リンク | Int J Biol Macromol / PubMed:36528147 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.74 Å |
構造データ | EMDB-34164, PDB-8gnh: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN/ANTIVIRAL PROTEIN / SARS-CoV-2 / Neutralizing monoclonal antibody / ANTIVIRAL PROTEIN / VIRAL PROTEIN-ANTIVIRAL PROTEIN complex |