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-Structure paper
タイトル | Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization. |
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ジャーナル・号・ページ | Cell Host Microbe, Vol. 29, Issue 5, Page 747-751.e4, Year 2021 |
掲載日 | 2021年5月12日 |
著者 | Pengfei Wang / Ryan G Casner / Manoj S Nair / Maple Wang / Jian Yu / Gabriele Cerutti / Lihong Liu / Peter D Kwong / Yaoxing Huang / Lawrence Shapiro / David D Ho / |
PubMed 要旨 | The emergence of SARS-CoV-2 variants has raised concerns about altered sensitivity to antibody-mediated immunity. The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody ...The emergence of SARS-CoV-2 variants has raised concerns about altered sensitivity to antibody-mediated immunity. The relative resistance of SARS-CoV-2 variants B.1.1.7 and B.1.351 to antibody neutralization has been recently investigated. We report that another emergent variant from Brazil, P.1, is not only refractory to multiple neutralizing monoclonal antibodies but also more resistant to neutralization by convalescent plasma and vaccinee sera. The magnitude of resistance is greater for monoclonal antibodies than vaccinee sera and evident with both pseudovirus and authentic P.1 virus. The cryoelectron microscopy structure of a soluble prefusion-stabilized spike reveals that the P.1 trimer adopts exclusively a conformation in which one of the receptor-binding domains is in the "up" position, which is known to facilitate binding to entry receptor ACE2. The functional impact of P.1 mutations thus appears to arise from local changes instead of global conformational alterations. The P.1 variant threatens current antibody therapies but less so protective vaccine efficacy. |
リンク | Cell Host Microbe / PubMed:33887205 / PubMed Central |
手法 | EM (単粒子) |
構造データ | EMDB-23718, PDB-7m8k: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN / Spike Glycoprotein |