7XNF

Structure of SARS-CoV-2 antibody P2C-1F11 with GX/P2V/2017 RBD

Summary for 7XNF

• Entry DOI: 10.2210/pdb7xnf/pdb
• Descriptor: P2C-1F11 Heavy Chain, P2C-1F11 Lambda chain, Spike protein S1, ... (4 entities in total)
• Functional Keywords: sars-cov-2, gx/p2v/2017, rbd, antibody, p2c1-f11, fab, viral protein
• Biological source: Homo sapiens; More
• Total number of polymer chains: 3
• Total formula weight: 71583.10

Authors

Jia, Y.F.,Chai, Y.,Wang, Q.H.,Gao, G.F. (deposition date: 2022-04-28, release date: 2023-01-11, Last modification date: 2023-11-29)

Primary citation

Jia, Y.,Niu, S.,Hu, Y.,Chai, Y.,Zheng, A.,Su, C.,Wu, L.,Han, P.,Han, P.,Lu, D.,Liu, Z.,Yan, X.,Tian, D.,Chen, Z.,Qi, J.,Tian, W.X.,Wang, Q.,Gao, G.F.
Cross-reaction of current available SARS-CoV-2 MAbs against the pangolin-origin coronavirus GX/P2V/2017.
Cell Rep, 41:111831-111831, 2022

PubMed Abstract: Since the identification of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the etiological agent of COVID-19, multiple SARS-CoV-2-related viruses have been characterized, including pangolin-origin GD/1/2019 and GX/P2V/2017. Our previous study indicated that both viruses have the potential to infect humans. Here, we find that CB6 (commercial name etesevimab), a COVID-19 therapeutic monoclonal antibody (MAb) developed by our group, efficiently inhibits GD/1/2019 but not GX/P2V/2017. A total of 50 SARS-CoV-2 MAbs divided into seven groups based on their receptor-binding domain (RBD) epitopes, together with the COVID-19 convalescent sera, are systematically screened for their cross-binding and cross-neutralizing properties against GX/P2V/2017. We find that GX/P2V/2017 displays substantial immune difference from SARS-CoV-2. Furthermore, we solve two complex structures of the GX/P2V/2017 RBD with MAbs belonging to RBD-1 and RBD-5, providing a structural basis for their different antigenicity. These results highlight the necessity for broad anti-coronavirus countermeasures and shed light on potential therapeutic targets.

PubMed: 36493785
DOI: 10.1016/j.celrep.2022.111831

Experimental method

X-RAY DIFFRACTION (2.79 Å)