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7VPY

Crystal structure of the neutralizing nanobody P86 against SARS-CoV-2

7VPY の概要
エントリーDOI10.2210/pdb7vpy/pdb
分子名称Nanobody, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
機能のキーワードsars-cov-2, immune system
由来する生物種Vicugna pacos
タンパク質・核酸の鎖数2
化学式量合計32216.01
構造登録者
主引用文献Maeda, R.,Fujita, J.,Konishi, Y.,Kazuma, Y.,Yamazaki, H.,Anzai, I.,Watanabe, T.,Yamaguchi, K.,Kasai, K.,Nagata, K.,Yamaoka, Y.,Miyakawa, K.,Ryo, A.,Shirakawa, K.,Sato, K.,Makino, F.,Matsuura, Y.,Inoue, T.,Imura, A.,Namba, K.,Takaori-Kondo, A.
A panel of nanobodies recognizing conserved hidden clefts of all SARS-CoV-2 spike variants including Omicron.
Commun Biol, 5:669-669, 2022
Cited by
PubMed Abstract: We are amid the historic coronavirus infectious disease 2019 (COVID-19) pandemic. Imbalances in the accessibility of vaccines, medicines, and diagnostics among countries, regions, and populations, and those in war crises, have been problematic. Nanobodies are small, stable, customizable, and inexpensive to produce. Herein, we present a panel of nanobodies that can detect the spike proteins of five SARS-CoV-2 variants of concern (VOCs) including Omicron. Here we show via ELISA, lateral flow, kinetic, flow cytometric, microscopy, and Western blotting assays that our nanobodies can quantify the spike variants. This panel of nanobodies broadly neutralizes viral infection caused by pseudotyped and authentic SARS-CoV-2 VOCs. Structural analyses show that the P86 clone targets epitopes that are conserved yet unclassified on the receptor-binding domain (RBD) and contacts the N-terminal domain (NTD). Human antibodies rarely access both regions; consequently, the clone buries hidden crevasses of SARS-CoV-2 spike proteins that go undetected by conventional antibodies.
PubMed: 35794202
DOI: 10.1038/s42003-022-03630-3
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.6 Å)
構造検証レポート
Validation report summary of 7vpy
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-08に公開中

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