7SN1
Structure of human SARS-CoV-2 neutralizing antibody C1C-A3 Fab
7SN1 の概要
| エントリーDOI | 10.2210/pdb7sn1/pdb |
| 分子名称 | neutralizing antibody C1C-A3 Fab heavy chain, neutralizing antibody C1C-A3 Fab light chain (3 entities in total) |
| 機能のキーワード | covid-19, sars-cov-2, neutralizing antibody, neutralization escape, immune system |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 52918.71 |
| 構造登録者 | |
| 主引用文献 | Nabel, K.G.,Clark, S.A.,Shankar, S.,Pan, J.,Clark, L.E.,Yang, P.,Coscia, A.,McKay, L.G.A.,Varnum, H.H.,Brusic, V.,Tolan, N.V.,Zhou, G.,Desjardins, M.,Turbett, S.E.,Kanjilal, S.,Sherman, A.C.,Dighe, A.,LaRocque, R.C.,Ryan, E.T.,Tylek, C.,Cohen-Solal, J.F.,Darcy, A.T.,Tavella, D.,Clabbers, A.,Fan, Y.,Griffiths, A.,Correia, I.R.,Seagal, J.,Baden, L.R.,Charles, R.C.,Abraham, J. Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain. Science, 375:eabl6251-eabl6251, 2022 Cited by PubMed Abstract: Many studies have examined the impact of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants on neutralizing antibody activity after they have become dominant strains. Here, we evaluate the consequences of further viral evolution. We demonstrate mechanisms through which the SARS-CoV-2 receptor binding domain (RBD) can tolerate large numbers of simultaneous antibody escape mutations and show that pseudotypes containing up to seven mutations, as opposed to the one to three found in previously studied variants of concern, are more resistant to neutralization by therapeutic antibodies and serum from vaccine recipients. We identify an antibody that binds the RBD core to neutralize pseudotypes for all tested variants but show that the RBD can acquire an N-linked glycan to escape neutralization. Our findings portend continued emergence of escape variants as SARS-CoV-2 adapts to humans. PubMed: 34855508DOI: 10.1126/science.abl6251 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.467 Å) |
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