Mary Wilson
Well-known member
Published: 04 November 2022
DOI https://doi.org/10.1038/s42003-022-04160-8
Jiangchao Xiang, Jie Su, Qiaoshuai Lan, Wenwen Zhao, Yu Zhou, Youwei Xu, Jun Niu, Shuai Xia, Qilian Qi, Sachdev Sidhu, Lu Lu, Shane Miersch & Bei Yang
Abstract
Understanding the antigenic signatures of all human coronaviruses (HCoVs) Spike (S) proteins is imperative for pan-HCoV epitopes identification and broadly effective vaccine development. To depict the currently elusive antigenic signatures of α-HCoVs S proteins, we isolated a panel of antibodies against the HCoV-229E S protein and characterized their epitopes and neutralizing potential. We found that the N-terminal domain of HCoV-229E S protein is antigenically dominant wherein an antigenic supersite is present and appears conserved in HCoV-NL63, which holds potential to serve as a pan-α-HCoVs epitope. In the receptor binding domain, a neutralizing epitope is captured in the end distal to the receptor binding site, reminiscent of the locations of the SARS-CoV-2 RBD cryptic epitopes. We also identified a neutralizing antibody that recognizes the connector domain, thus representing the first S2-directed neutralizing antibody against α-HCoVs. The unraveled HCoVs S proteins antigenic similarities and variances among genera highlight the challenges faced by pan-HCoV vaccine design while supporting the feasibility of broadly effective vaccine development against a subset of HCoVs.
https://www.nature.com/articles/s42003-022-04160-8#citeas
DOI https://doi.org/10.1038/s42003-022-04160-8
Jiangchao Xiang, Jie Su, Qiaoshuai Lan, Wenwen Zhao, Yu Zhou, Youwei Xu, Jun Niu, Shuai Xia, Qilian Qi, Sachdev Sidhu, Lu Lu, Shane Miersch & Bei Yang
Abstract
Understanding the antigenic signatures of all human coronaviruses (HCoVs) Spike (S) proteins is imperative for pan-HCoV epitopes identification and broadly effective vaccine development. To depict the currently elusive antigenic signatures of α-HCoVs S proteins, we isolated a panel of antibodies against the HCoV-229E S protein and characterized their epitopes and neutralizing potential. We found that the N-terminal domain of HCoV-229E S protein is antigenically dominant wherein an antigenic supersite is present and appears conserved in HCoV-NL63, which holds potential to serve as a pan-α-HCoVs epitope. In the receptor binding domain, a neutralizing epitope is captured in the end distal to the receptor binding site, reminiscent of the locations of the SARS-CoV-2 RBD cryptic epitopes. We also identified a neutralizing antibody that recognizes the connector domain, thus representing the first S2-directed neutralizing antibody against α-HCoVs. The unraveled HCoVs S proteins antigenic similarities and variances among genera highlight the challenges faced by pan-HCoV vaccine design while supporting the feasibility of broadly effective vaccine development against a subset of HCoVs.
https://www.nature.com/articles/s42003-022-04160-8#citeas