7N1V

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

7N1V の概要

• エントリーDOI: 10.2210/pdb7n1v/pdb
• EMDBエントリー: 24124
• 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-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: 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: 453018.22

構造登録者

Zhang, J.,Cai, Y.F.,Xiao, T.S.,Rawson, S.,Peng, H.Q.,Sterling, S.M.,Walsh Jr, R.M.,Volloch, S.R.,Chen, B. (登録日: 2021-05-28, 公開日: 2021-07-07, 最終更新日: 2024-10-30)

主引用文献

Cai, Y.,Zhang, J.,Xiao, T.,Lavine, C.L.,Rawson, S.,Peng, H.,Zhu, H.,Anand, K.,Tong, P.,Gautam, A.,Lu, S.,Sterling, S.M.,Walsh Jr., R.M.,Rits-Volloch, S.,Lu, J.,Wesemann, D.R.,Yang, W.,Seaman, M.S.,Chen, B.
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.
Science, 373:642-648, 2021

PubMed Abstract: Several fast-spreading variants of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) have become the dominant circulating strains in the COVID-19 pandemic. We report here cryo-electron microscopy structures of the full-length spike (S) trimers of the B.1.1.7 and B.1.351 variants, as well as their biochemical and antigenic properties. Amino acid substitutions in the B.1.1.7 protein increase both the accessibility of its receptor binding domain and the binding affinity for receptor angiotensin-converting enzyme 2 (ACE2). The enhanced receptor engagement may account for the increased transmissibility. The B.1.351 variant has evolved to reshape antigenic surfaces of the major neutralizing sites on the S protein, making it resistant to some potent neutralizing antibodies. These findings provide structural details on how SARS-CoV-2 has evolved to enhance viral fitness and immune evasion.

PubMed: 34168070
DOI: 10.1126/science.abi9745

実験手法

ELECTRON MICROSCOPY (3.21 Å)