7B27 の概要
| エントリーDOI | 10.2210/pdb7b27/pdb |
| 分子名称 | Surface glycoprotein, neutralizing nanobody NM1230, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| 機能のキーワード | sars-cov2, receptor binding domain, complex structure, neutralizing nanobody, viral protein |
| 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 | 4 |
| 化学式量合計 | 81319.46 |
| 構造登録者 | |
| 主引用文献 | Wagner, T.R.,Ostertag, E.,Kaiser, P.D.,Gramlich, M.,Ruetalo, N.,Junker, D.,Haering, J.,Traenkle, B.,Becker, M.,Dulovic, A.,Schweizer, H.,Nueske, S.,Scholz, A.,Zeck, A.,Schenke-Layland, K.,Nelde, A.,Strengert, M.,Walz, J.S.,Zocher, G.,Stehle, T.,Schindler, M.,Schneiderhan-Marra, N.,Rothbauer, U. NeutrobodyPlex-monitoring SARS-CoV-2 neutralizing immune responses using nanobodies. Embo Rep., 22:e52325-e52325, 2021 Cited by PubMed Abstract: In light of the COVID-19 pandemic, there is an ongoing need for diagnostic tools to monitor the immune status of large patient cohorts and the effectiveness of vaccination campaigns. Here, we present 11 unique nanobodies (Nbs) specific for the SARS-CoV-2 spike receptor-binding domain (RBD), of which 8 Nbs potently inhibit the interaction of RBD with angiotensin-converting enzyme 2 (ACE2) as the major viral docking site. Following detailed epitope mapping and structural analysis, we select two inhibitory Nbs, one of which binds an epitope inside and one of which binds an epitope outside the RBD:ACE2 interface. Based on these, we generate a biparatopic nanobody (bipNb) with viral neutralization efficacy in the picomolar range. Using bipNb as a surrogate, we establish a competitive multiplex binding assay ("NeutrobodyPlex") for detailed analysis of the presence and performance of neutralizing RBD-binding antibodies in serum of convalescent or vaccinated patients. We demonstrate that NeutrobodyPlex enables high-throughput screening and detailed analysis of neutralizing immune responses in infected or vaccinated individuals, to monitor immune status or to guide vaccine design. PubMed: 33904225DOI: 10.15252/embr.202052325 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.902 Å) |
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