7JVB

Crystal structure of the SARS-CoV-2 spike receptor-binding domain (RBD) with nanobody Nb20

7JVB の概要

• エントリーDOI: 10.2210/pdb7jvb/pdb
• 分子名称: Spike protein S1, Nanobody Nb20, CACODYLATE ION (3 entities in total)
• 機能のキーワード: sars-cov-2, covid-19, nanobody, spike protein, receptor-binding domain, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2, COVID-19 virus); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 76012.83

構造登録者

Xiang, Y.,Xiao, Z.,Liu, H.,Sang, Z.,Schneidman-Duhovny, D.,Zhang, C.,Shi, Y. (登録日: 2020-08-20, 公開日: 2020-12-02, 最終更新日: 2024-11-20)

主引用文献

Xiang, Y.,Nambulli, S.,Xiao, Z.,Liu, H.,Sang, Z.,Duprex, W.P.,Schneidman-Duhovny, D.,Zhang, C.,Shi, Y.
Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2.
Science, 370:1479-1484, 2020

PubMed Abstract: Cost-effective, efficacious therapeutics are urgently needed to combat the COVID-19 pandemic. In this study, we used camelid immunization and proteomics to identify a large repertoire of highly potent neutralizing nanobodies (Nbs) to the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein receptor binding domain (RBD). We discovered Nbs with picomolar to femtomolar affinities that inhibit viral infection at concentrations below the nanograms-per-milliliter level, and we determined a structure of one of the most potent Nbs in complex with the RBD. Structural proteomics and integrative modeling revealed multiple distinct and nonoverlapping epitopes and indicated an array of potential neutralization mechanisms. We bioengineered multivalent Nb constructs that achieved ultrahigh neutralization potency (half-maximal inhibitory concentration as low as 0.058 ng/ml) and may prevent mutational escape. These thermostable Nbs can be rapidly produced in bulk from microbes and resist lyophilization and aerosolization.

PubMed: 33154108
DOI: 10.1126/science.abe4747

実験手法

X-RAY DIFFRACTION (3.287 Å)