7X1M

The complex structure of Omicron BA.1 RBD with BD604, S309,and S304

Summary for 7X1M

• Entry DOI: 10.2210/pdb7x1m/pdb
• EMDB information: 32944
• Descriptor: S309 Fab heavy chain, S309 Fab light chain, BD-604 Fab heavy chain, ... (8 entities in total)
• Functional Keywords: antibody viral protein complex, viral protein, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 7
• Total formula weight: 165881.03

Authors

Huang, M.,Xie, Y.F.,Qi, J.X. (deposition date: 2022-02-24, release date: 2022-07-06, Last modification date: 2024-10-30)

Primary citation

Huang, M.,Wu, L.,Zheng, A.,Xie, Y.,He, Q.,Rong, X.,Han, P.,Du, P.,Han, P.,Zhang, Z.,Zhao, R.,Jia, Y.,Li, L.,Bai, B.,Hu, Z.,Hu, S.,Niu, S.,Hu, Y.,Liu, H.,Liu, B.,Cui, K.,Li, W.,Zhao, X.,Liu, K.,Qi, J.,Wang, Q.,Gao, G.F.
Atlas of currently available human neutralizing antibodies against SARS-CoV-2 and escape by Omicron sub-variants BA.1/BA.1.1/BA.2/BA.3.
Immunity, 55:1501-1514.e3, 2022

PubMed Abstract: SARS-CoV-2 Omicron variant has presented significant challenges to current antibodies and vaccines. Herein, we systematically compared the efficacy of 50 human monoclonal antibodies (mAbs), covering the seven identified epitope classes of the SARS-CoV-2 RBD, against Omicron sub-variants BA.1, BA.1.1, BA.2, and BA.3. Binding and pseudovirus-based neutralizing assays revealed that 37 of the 50 mAbs lost neutralizing activities, whereas the others displayed variably decreased activities against the four Omicron sub-variants. BA.2 was found to be more sensitive to RBD-5 antibodies than the other sub-variants. Furthermore, a quaternary complex structure of BA.1 RBD with three mAbs showing different neutralizing potencies against Omicron provided a basis for understanding the immune evasion of Omicron sub-variants and revealed the lack of G446S mutation accounting for the sensitivity of BA.2 to RBD-5 mAbs. Our results may guide the application of the available mAbs and facilitate the development of universal therapeutic antibodies and vaccines against COVID-19.

PubMed: 35777362
DOI: 10.1016/j.immuni.2022.06.005

Experimental method

ELECTRON MICROSCOPY (2.74 Å)