7SI2
Crystal structure of neutralizing antibody 10-28 in complex with SARS-CoV-2 spike receptor binding domain (RBD)
Summary for 7SI2
| Entry DOI | 10.2210/pdb7si2/pdb |
| Descriptor | 10-28 Light Chain, 10-28 Heavy Chain, Spike protein S1, ... (4 entities in total) |
| Functional Keywords | covid-19, sars-cov-2, viral protein, spike glycoprotein, receptor binding protein, rbd, neutralizing antibody, 10-28, fab, viral protein-immune system complex, viral protein/immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 9 |
| Total formula weight | 223704.94 |
| Authors | Reddem, E.R.,Shapiro, L. (deposition date: 2021-10-12, release date: 2022-04-27, Last modification date: 2024-11-06) |
| Primary citation | Liu, L.,Iketani, S.,Guo, Y.,Reddem, E.R.,Casner, R.G.,Nair, M.S.,Yu, J.,Chan, J.F.,Wang, M.,Cerutti, G.,Li, Z.,Morano, N.C.,Castagna, C.D.,Corredor, L.,Chu, H.,Yuan, S.,Poon, V.K.,Chan, C.C.,Chen, Z.,Luo, Y.,Cunningham, M.,Chavez, A.,Yin, M.T.,Perlin, D.S.,Tsuji, M.,Yuen, K.Y.,Kwong, P.D.,Sheng, Z.,Huang, Y.,Shapiro, L.,Ho, D.D. An antibody class with a common CDRH3 motif broadly neutralizes sarbecoviruses. Sci Transl Med, 14:eabn6859-eabn6859, 2022 Cited by PubMed Abstract: The devastation caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has made clear the importance of pandemic preparedness. To address future zoonotic outbreaks due to related viruses in the sarbecovirus subgenus, we identified a human monoclonal antibody, 10-40, that neutralized or bound all sarbecoviruses tested in vitro and protected against SARS-CoV-2 and SARS-CoV in vivo. Comparative studies with other receptor-binding domain (RBD)-directed antibodies showed 10-40 to have the greatest breadth against sarbecoviruses, suggesting that 10-40 is a promising agent for pandemic preparedness. Moreover, structural analyses on 10-40 and similar antibodies not only defined an epitope cluster in the inner face of the RBD that is well conserved among sarbecoviruses but also uncovered a distinct antibody class with a common CDRH3 motif. Our analyses also suggested that elicitation of this class of antibodies may not be overly difficult, an observation that bodes well for the development of a pan-sarbecovirus vaccine. PubMed: 35438546DOI: 10.1126/scitranslmed.abn6859 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
Download full validation report
