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-Structure paper
タイトル | Structural and functional impact by SARS-CoV-2 Omicron spike mutations. |
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ジャーナル・号・ページ | Cell Rep, Vol. 39, Issue 4, Page 110729, Year 2022 |
掲載日 | 2022年4月26日 |
著者 | Jun Zhang / Yongfei Cai / Christy L Lavine / Hanqin Peng / Haisun Zhu / Krishna Anand / Pei Tong / Avneesh Gautam / Megan L Mayer / Sophia Rits-Volloch / Shaowei Wang / Piotr Sliz / Duane R Wesemann / Wei Yang / Michael S Seaman / Jianming Lu / Tianshu Xiao / Bing Chen / |
PubMed 要旨 | The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. ...The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. We report here structural, functional, and antigenic properties of its full-length spike (S) protein with a native sequence in comparison with those of previously prevalent variants. Omicron S requires a substantially higher level of host receptor ACE2 for efficient membrane fusion than other variants, possibly explaining its unexpected cellular tropism. Mutations not only remodel the antigenic structure of the N-terminal domain of the S protein but also alter the surface of the receptor-binding domain in a way not seen in other variants, consistent with its remarkable resistance to neutralizing antibodies. These results suggest that Omicron S has acquired an extraordinary ability to evade host immunity by excessive mutations, which also compromise its fusogenic capability. |
リンク | Cell Rep / PubMed:35452593 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.1 - 3.4 Å |
構造データ | EMDB-26021, PDB-7tnw: EMDB-26029, PDB-7to4: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN |