7WUE
Crystal structure of SARS-CoV-2 Receptor Binding Domain in complex with the monoclonal antibody m31A7
7WUE の概要
| エントリーDOI | 10.2210/pdb7wue/pdb |
| 分子名称 | Spike protein S1, m31A7 Fab HEAVY CHAIN, m31A7 Fab LIGHT CHAIN, ... (5 entities in total) |
| 機能のキーワード | sars-cov-2, spike, receptor binding domain, m31a7, monoclonal antibody, viral protein, viral protein-immune system complex, viral protein/immune system |
| 由来する生物種 | Severe acute respiratory syndrome coronavirus 2 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 150725.26 |
| 構造登録者 | |
| 主引用文献 | Huang, H.Y.,Liao, H.Y.,Chen, X.,Wang, S.W.,Cheng, C.W.,Shahed-Al-Mahmud, M.,Liu, Y.M.,Mohapatra, A.,Chen, T.H.,Lo, J.M.,Wu, Y.M.,Ma, H.H.,Chang, Y.H.,Tsai, H.Y.,Chou, Y.C.,Hsueh, Y.P.,Tsai, C.Y.,Huang, P.Y.,Chang, S.Y.,Chao, T.L.,Kao, H.C.,Tsai, Y.M.,Chen, Y.H.,Wu, C.Y.,Jan, J.T.,Cheng, T.R.,Lin, K.I.,Ma, C.,Wong, C.H. Vaccination with SARS-CoV-2 spike protein lacking glycan shields elicits enhanced protective responses in animal models. Sci Transl Med, 14:eabm0899-eabm0899, 2022 Cited by PubMed Abstract: A major challenge to end the pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is to develop a broadly protective vaccine that elicits long-term immunity. As the key immunogen, the viral surface spike (S) protein is frequently mutated, and conserved epitopes are shielded by glycans. Here, we revealed that S protein glycosylation has site-differential effects on viral infectivity. We found that S protein generated by lung epithelial cells has glycoforms associated with increased infectivity. Compared to the fully glycosylated S protein, immunization of S protein with N-glycans trimmed to the mono-GlcNAc-decorated state (S) elicited stronger immune responses and better protection for human angiotensin-converting enzyme 2 (hACE2) transgenic mice against variants of concern (VOCs). In addition, a broadly neutralizing monoclonal antibody was identified from S-immunized mice that could neutralize wild-type SARS-CoV-2 and VOCs with subpicomolar potency. Together, these results demonstrate that removal of glycan shields to better expose the conserved sequences has the potential to be an effective and simple approach for developing a broadly protective SARS-CoV-2 vaccine. PubMed: 35230146DOI: 10.1126/scitranslmed.abm0899 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






