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.
【초록키워드】 neutralizing antibody, Vaccine development, S protein, spike, feasibility, Vaccine design, Receptor binding domain, Protein, Epitopes, RBD, understanding, HCoV-229E, Neutralizing, epitope, N-terminal domain, HCoV-NL63, similarity, antigenic, domain, S proteins, receptor binding site, dominant, effective, highlight, human coronavirus, conserved, characterized, appear, recognize, imperative, representing, subset, distal, panel of antibody, the SARS-CoV-2, 【제목키워드】 Spike protein, reveal,