8GTQ
cryo-EM structure of Omicron BA.5 S protein in complex with S2L20
8GTQ の概要
エントリーDOI | 10.2210/pdb8gtq/pdb |
EMDBエントリー | 34263 |
分子名称 | Spike glycoprotein, heavy chain of S2L20, light chain of S2L20, ... (6 entities in total) |
機能のキーワード | sars-cov-2, viral protein, viral protein-immune system complex, viral protein/immune system |
由来する生物種 | Severe acute respiratory syndrome coronavirus 2 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 515987.97 |
構造登録者 | |
主引用文献 | Chi, X.,Xia, L.,Zhang, G.,Chi, X.,Huang, B.,Zhang, Y.,Chen, Z.,Han, J.,Wu, L.,Li, Z.,Sun, H.,Huang, P.,Yu, C.,Chen, W.,Zhou, Q. Comprehensive structural analysis reveals broad-spectrum neutralizing antibodies against SARS-CoV-2 Omicron variants. Cell Discov, 9:37-37, 2023 Cited by PubMed Abstract: The pandemic of COVID-19 caused by SARS-CoV-2 continues to spread around the world. Mutant strains of SARS-CoV-2 are constantly emerging. At present, Omicron variants have become mainstream. In this work, we carried out a systematic and comprehensive analysis of the reported spike protein antibodies, counting the epitopes and genotypes of these antibodies. We further comprehensively analyzed the impact of Omicron mutations on antibody epitopes and classified these antibodies according to their binding patterns. We found that the epitopes of the H-RBD class antibodies were significantly less affected by Omicron mutations than other classes. Binding and virus neutralization experiments showed that such antibodies could effectively inhibit the immune escape of Omicron. Cryo-EM results showed that this class of antibodies utilized a conserved mechanism to neutralize SARS-CoV-2. Our results greatly help us deeply understand the impact of Omicron mutations. Meanwhile, it also provides guidance and insights for developing Omicron antibodies and vaccines. PubMed: 37015915DOI: 10.1038/s41421-023-00535-1 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.1 Å) |
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