8GTP

cryo-EM structure of Omicron BA.5 S protein in complex with XGv289

Summary for 8GTP

• Entry DOI: 10.2210/pdb8gtp/pdb
• EMDB information: 34261
• Descriptor: Spike glycoprotein, heavy chain of XGv289, light chain of XGv289, ... (5 entities in total)
• Functional Keywords: sars-cov-2, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2); More
• Total number of polymer chains: 9
• Total formula weight: 512975.26

Authors

Xia, X.Y.,Zhang, Y.Y.,Chi, X.M.,Huang, B.D.,Wu, L.S.,Zhou, Q. (deposition date: 2022-09-08, release date: 2023-07-12)

Primary citation

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

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: 37015915
DOI: 10.1038/s41421-023-00535-1

Experimental method

ELECTRON MICROSCOPY (3.1 Å)