A key linear epitope for a potent neutralizing antibody to SARS-CoV-2 S-RBD
Li, T.; Han, X.; Wang, Y.; Gu, C.; Wang, J.; Hu, C.; Li, S.; Wang, K.; Luo, F.; Huang, J.; Long, Y.; Song, S.; Wang, W.; Hu, J.; Wu, R.; Mu, S.; Hao, Y.; Chen, Q.; Gao, F.; Shen, M.; Long, S.; Gong, F.; Li, L.; Wu, Y.; Xu, W.; Cai, X.; Qu, D.; Yuan, Z.; Gao, Q.; Zhang, G.; He, C.; Nai, Y.; Deng, K.; Du, L.; Tang, N.; Xie, Y.; Huang, A.; Jin, A.
Show abstract
The spread of SARS-CoV-2 confers a serious threat to the public health without effective intervention strategies1-3. Its variant carrying mutated Spike (S) protein D614G (SD614G) has become the most prevalent form in the current global pandemic4,5. We have identified a large panel of potential neutralizing antibodies (NAbs) targeting the receptor-binding domain (RBD) of SARS-CoV-2 S6. Here, we focused on the top 20 potential NAbs for the mechanism study. Of them, the top 4 NAbs could individually neutralize both authentic SARS-CoV-2 and SD614G pseudovirus efficiently. Our epitope mapping revealed that 16/20 potent NAbs overlapped the same steric epitope. Excitingly, we found that one of these potent NAbs (58G6) exclusively bound to a linear epitope on S-RBD (termed as 58G6e), and the interaction of 58G6e and the recombinant ACE2 could be blocked by 58G6. We confirmed that 58G6e represented a key site of vulnerability on S-RBD and it could positively react with COVID-19 convalescent patients plasma. We are the first, as far as we know, to provide direct evidences of a linear epitope that can be recognized by a potent NAb against SARS-CoV-2 S-RBD. This study paves the way for the applications of these NAbs and the potential safe and effective vaccine design.
Matching journals
The top 4 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Ultrapotent SARS-CoV-2 neutralizing antibodies with protective efficacy against newly emerged mutational variants 99%
- Distinct mechanisms for TMPRSS2 expression explain organ-specific inhibition of SARS-CoV-2 infection by enzalutamide 97%
- Sarbecovirus RBD indels and specific residues dictating ACE2 multi-species adaptiveness 97%
Similar papers in this journal
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.