7TE1
SARS-CoV-2 Receptor Binding Domain in Complex with Ab17
Summary for 7TE1
| Entry DOI | 10.2210/pdb7te1/pdb |
| Descriptor | Ab17 heavy chain, Ab17 light chain, Spike protein S1 (3 entities in total) |
| Functional Keywords | antibody-antigen complex, sars-cov-2, receptor binding domain, immune system, immune system-viral protein complex, immune system/viral protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 6 |
| Total formula weight | 142222.50 |
| Authors | Hauser, B.M.,Schmidt, A.G. (deposition date: 2022-01-03, release date: 2022-03-30, Last modification date: 2024-11-20) |
| Primary citation | Hauser, B.M.,Sangesland, M.,St Denis, K.J.,Lam, E.C.,Case, J.B.,Windsor, I.W.,Feldman, J.,Caradonna, T.M.,Kannegieter, T.,Diamond, M.S.,Balazs, A.B.,Lingwood, D.,Schmidt, A.G. Rationally designed immunogens enable immune focusing following SARS-CoV-2 spike imprinting. Cell Rep, 38:110561-110561, 2022 Cited by PubMed Abstract: Eliciting antibodies to surface-exposed viral glycoproteins can generate protective responses that control and prevent future infections. Targeting conserved sites may reduce the likelihood of viral escape and limit the spread of related viruses with pandemic potential. Here we leverage rational immunogen design to focus humoral responses on conserved epitopes. Using glycan engineering and epitope scaffolding in boosting immunogens, we focus murine serum antibody responses to conserved receptor binding motif (RBM) and receptor binding domain (RBD) epitopes following severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike imprinting. Although all engineered immunogens elicit a robust SARS-CoV-2-neutralizing serum response, RBM-focusing immunogens exhibit increased potency against related sarbecoviruses, SARS-CoV, WIV1-CoV, RaTG13-CoV, and SHC014-CoV; structural characterization of representative antibodies defines a conserved epitope. RBM-focused sera confer protection against SARS-CoV-2 challenge. Thus, RBM focusing is a promising strategy to elicit breadth across emerging sarbecoviruses without compromising SARS-CoV-2 protection. These engineering strategies are adaptable to other viral glycoproteins for targeting conserved epitopes. PubMed: 35303475DOI: 10.1016/j.celrep.2022.110561 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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