tetano
Editor, Senior Moderator
Cell Rep
. 2022 Nov 29;111831.
doi: 10.1016/j.celrep.2022.111831. Online ahead of print.
Cross-reaction of current available SARS-CoV-2 MAbs against the pangolin-origin coronavirus GX/P2V/2017
Yunfei Jia[SUP] 1 [/SUP], Sheng Niu[SUP] 2 [/SUP], Yu Hu[SUP] 3 [/SUP], Yan Chai[SUP] 4 [/SUP], Anqi Zheng[SUP] 5 [/SUP], Chao Su[SUP] 6 [/SUP], Lili Wu[SUP] 4 [/SUP], Pengcheng Han[SUP] 7 [/SUP], Pu Han[SUP] 4 [/SUP], Dan Lu[SUP] 8 [/SUP], Zhimin Liu[SUP] 2 [/SUP], Xinxin Yan[SUP] 1 [/SUP], Di Tian[SUP] 9 [/SUP], Zhihai Chen[SUP] 9 [/SUP], Jianxun Qi[SUP] 4 [/SUP], Wen-Xia Tian[SUP] 10 [/SUP], Qihui Wang[SUP] 11 [/SUP], George Fu Gao[SUP] 12 [/SUP]
Affiliations
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.
Keywords: CP: Immunology; CP: Microbiology; SARS-CoV-2; immune difference; monoclonal antibody; pangolin CoVs.
. 2022 Nov 29;111831.
doi: 10.1016/j.celrep.2022.111831. Online ahead of print.
Cross-reaction of current available SARS-CoV-2 MAbs against the pangolin-origin coronavirus GX/P2V/2017
Yunfei Jia[SUP] 1 [/SUP], Sheng Niu[SUP] 2 [/SUP], Yu Hu[SUP] 3 [/SUP], Yan Chai[SUP] 4 [/SUP], Anqi Zheng[SUP] 5 [/SUP], Chao Su[SUP] 6 [/SUP], Lili Wu[SUP] 4 [/SUP], Pengcheng Han[SUP] 7 [/SUP], Pu Han[SUP] 4 [/SUP], Dan Lu[SUP] 8 [/SUP], Zhimin Liu[SUP] 2 [/SUP], Xinxin Yan[SUP] 1 [/SUP], Di Tian[SUP] 9 [/SUP], Zhihai Chen[SUP] 9 [/SUP], Jianxun Qi[SUP] 4 [/SUP], Wen-Xia Tian[SUP] 10 [/SUP], Qihui Wang[SUP] 11 [/SUP], George Fu Gao[SUP] 12 [/SUP]
Affiliations
- PMID: 36493785
- DOI: 10.1016/j.celrep.2022.111831
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.
Keywords: CP: Immunology; CP: Microbiology; SARS-CoV-2; immune difference; monoclonal antibody; pangolin CoVs.