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-Structure paper
タイトル | Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein. |
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ジャーナル・号・ページ | bioRxiv, Year 2021 |
掲載日 | 2021年1月20日 |
著者 | Naveenchandra Suryadevara / Swathi Shrihari / Pavlo Gilchuk / Laura A VanBlargan / Elad Binshtein / Seth J Zost / Rachel S Nargi / Rachel E Sutton / Emma S Winkler / Elaine C Chen / Mallorie E Fouch / Edgar Davidson / Benjamin J Doranz / Robert H Carnahan / Larissa B Thackray / Michael S Diamond / James E Crowe |
PubMed 要旨 | Most human monoclonal antibodies (mAbs) neutralizing SARS-CoV-2 recognize the spike (S) protein receptor-binding domain and block virus interactions with the cellular receptor angiotensin-converting ...Most human monoclonal antibodies (mAbs) neutralizing SARS-CoV-2 recognize the spike (S) protein receptor-binding domain and block virus interactions with the cellular receptor angiotensin-converting enzyme 2. We describe a panel of human mAbs binding to diverse epitopes on the N-terminal domain (NTD) of S protein from SARS-CoV-2 convalescent donors and found a minority of these possessed neutralizing activity. Two mAbs (COV2-2676 and COV2-2489) inhibited infection of authentic SARS-CoV-2 and recombinant VSV/SARS-CoV-2 viruses. We mapped their binding epitopes by alanine-scanning mutagenesis and selection of functional SARS-CoV-2 S neutralization escape variants. Mechanistic studies showed that these antibodies neutralize in part by inhibiting a post-attachment step in the infection cycle. COV2-2676 and COV2-2489 offered protection either as prophylaxis or therapy, and Fc effector functions were required for optimal protection. Thus, natural infection induces a subset of potent NTD-specific mAbs that leverage neutralizing and Fc-mediated activities to protect against SARS-CoV-2 infection using multiple functional attributes. |
リンク | bioRxiv / PubMed:33501445 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 21.0 - 25.0 Å |
構造データ | EMDB-23154: EMDB-23155: |
由来 |
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