7M8K

Cryo-EM structure of Brazil (P.1) SARS-CoV-2 spike glycoprotein variant in the prefusion state (1 RBD up)

7M8K の概要

• エントリーDOI: 10.2210/pdb7m8k/pdb
• EMDBエントリー: 23718
• 分子名称: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: spike glycoprotein, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 429062.33

構造登録者

Casner, R.G.,Cerutti, G.,Shapiro, L.,Ho, D.D. (登録日: 2021-03-29, 公開日: 2021-05-05, 最終更新日: 2025-03-19)

主引用文献

Wang, P.,Casner, R.G.,Nair, M.S.,Wang, M.,Yu, J.,Cerutti, G.,Liu, L.,Kwong, P.D.,Huang, Y.,Shapiro, L.,Ho, D.D.
Increased resistance of SARS-CoV-2 variant P.1 to antibody neutralization.
Cell Host Microbe, 29:747-, 2021

PubMed Abstract: 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.

PubMed: 33887205
DOI: 10.1016/j.chom.2021.04.007

実験手法

ELECTRON MICROSCOPY (3.8 Å)