7TE1
SARS-CoV-2 Receptor Binding Domain in Complex with Ab17
7TE1 の概要
| エントリーDOI | 10.2210/pdb7te1/pdb |
| 分子名称 | Ab17 heavy chain, Ab17 light chain, Spike protein S1 (3 entities in total) |
| 機能のキーワード | antibody-antigen complex, sars-cov-2, receptor binding domain, immune system, immune system-viral protein complex, immune system/viral protein |
| 由来する生物種 | Homo sapiens 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 142222.50 |
| 構造登録者 | |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.5 Å) |
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