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-Structure paper
タイトル | Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants. |
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ジャーナル・号・ページ | Science, Vol. 373, Issue 6555, Page 642-648, Year 2021 |
掲載日 | 2021年8月6日 |
著者 | Yongfei Cai / Jun Zhang / Tianshu Xiao / Christy L Lavine / Shaun Rawson / Hanqin Peng / Haisun Zhu / Krishna Anand / Pei Tong / Avneesh Gautam / Shen Lu / Sarah M Sterling / Richard M Walsh / Sophia Rits-Volloch / Jianming Lu / Duane R Wesemann / Wei Yang / Michael S Seaman / Bing Chen / |
PubMed 要旨 | 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 ...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. |
リンク | Science / PubMed:34168070 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.9 - 4.3 Å |
構造データ | EMDB-24121, PDB-7n1q: EMDB-24122, PDB-7n1t: EMDB-24123, PDB-7n1u: EMDB-24124, PDB-7n1v: EMDB-24125, PDB-7n1w: EMDB-24126, PDB-7n1x: EMDB-24127, PDB-7n1y: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN |