7N5H
Cryo-EM structure of broadly neutralizing antibody 2-36 in complex with prefusion SARS-CoV-2 spike glycoprotein
7N5H の概要
エントリーDOI | 10.2210/pdb7n5h/pdb |
EMDBエントリー | 24190 |
分子名称 | Spike glycoprotein, 2-36 Fab heavy chain, 2-36 Fab light chain, ... (5 entities in total) |
機能のキーワード | sars-cov-2, viral spike, trimer, glycoprotein, neutralizing antibody fab, viral protein-immune system complex, viral protein/immune system |
由来する生物種 | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) 詳細 |
タンパク質・核酸の鎖数 | 9 |
化学式量合計 | 513329.87 |
構造登録者 | |
主引用文献 | Wang, P.,Casner, R.G.,Nair, M.S.,Yu, J.,Guo, Y.,Wang, M.,Chan, J.F.,Cerutti, G.,Iketani, S.,Liu, L.,Sheng, Z.,Chen, Z.,Yuen, K.Y.,Kwong, P.D.,Huang, Y.,Shapiro, L.,Ho, D.D. A monoclonal antibody that neutralizes SARS-CoV-2 variants, SARS-CoV, and other sarbecoviruses. Emerg Microbes Infect, 11:147-157, 2022 Cited by PubMed Abstract: The repeated emergence of highly pathogenic human coronaviruses as well as their evolving variants highlight the need to develop potent and broad-spectrum antiviral therapeutics and vaccines. By screening monoclonal antibodies (mAbs) isolated from COVID-19-convalescent patients, we found one mAb, 2-36, with cross-neutralizing activity against SARS-CoV. We solved the cryo-EM structure of 2-36 in complex with SARS-CoV-2 or SARS-CoV spike, revealing a highly conserved epitope in the receptor-binding domain (RBD). Antibody 2-36 neutralized not only all current circulating SARS-CoV-2 variants and SARS-COV, but also a panel of bat and pangolin sarbecoviruses that can use human angiotensin-converting enzyme 2 (ACE2) as a receptor. We selected 2-36-escape viruses and confirmed that K378 T in SARS-CoV-2 RBD led to viral resistance. Taken together, 2-36 represents a strategic reserve drug candidate for the prevention and treatment of possible diseases caused by pre-emergent SARS-related coronaviruses. Its epitope defines a promising target for the development of a pan-sarbecovirus vaccine. PubMed: 34836485DOI: 10.1080/22221751.2021.2011623 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.24 Å) |
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