8HGL

SARS-CoV-2 spike in complex with neutralizing antibody NIV-11

8HGL の概要

• エントリーDOI: 10.2210/pdb8hgl/pdb
• EMDBエントリー: 34741
• 分子名称: Spike glycoprotein, NIV-11 Fab heavy chain, NIV-11 Fab light chain, ... (5 entities in total)
• 機能のキーワード: complex, viral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV,SARS-CoV-2); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 582265.15

構造登録者

Moriyama, S.,Anraku, Y.,Muranishi, S.,Adachi, Y.,Kuroda, D.,Higuchi, Y.,Kotaki, R.,Tonouchi, K.,Yumoto, K.,Suzuki, T.,Kita, S.,Someya, T.,Fukuhara, H.,Kuroda, Y.,Yamamoto, T.,Onodera, T.,Fukushi, S.,Maeda, K.,Nakamura-Uchiyama, F.,Hashiguchi, T.,Hoshino, A.,Maenaka, K.,Takahashi, Y. (登録日: 2022-11-15, 公開日: 2023-10-25, 最終更新日: 2024-10-23)

主引用文献

Moriyama, S.,Anraku, Y.,Taminishi, S.,Adachi, Y.,Kuroda, D.,Kita, S.,Higuchi, Y.,Kirita, Y.,Kotaki, R.,Tonouchi, K.,Yumoto, K.,Suzuki, T.,Someya, T.,Fukuhara, H.,Kuroda, Y.,Yamamoto, T.,Onodera, T.,Fukushi, S.,Maeda, K.,Nakamura-Uchiyama, F.,Hashiguchi, T.,Hoshino, A.,Maenaka, K.,Takahashi, Y.
Structural delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants.
Nat Commun, 14:4198-4198, 2023

PubMed Abstract: SARS-CoV-2 Omicron subvariants have evolved to evade receptor-binding site (RBS) antibodies that exist in diverse individuals as public antibody clones. We rationally selected RBS antibodies resilient to mutations in emerging Omicron subvariants. Y489 was identified as a site of virus vulnerability and a common footprint of broadly neutralizing antibodies against the subvariants. Multiple Y489-binding antibodies were encoded by public clonotypes and additionally recognized F486, potentially accounting for the emergence of Omicron subvariants harboring the F486V mutation. However, a subclass of antibodies broadly neutralized BA.4/BA.5 variants via hydrophobic binding sites of rare clonotypes along with high mutation-resilience under escape mutation screening. A computationally designed antibody based on one of the Y489-binding antibodies, NIV-10/FD03, was able to bind XBB with any 486 mutation and neutralized XBB.1.5. The structural basis for the mutation-resilience of this Y489-binding antibody group may provide important insights into the design of therapeutics resistant to viral escape.

PubMed: 37452031
DOI: 10.1038/s41467-023-39890-8

実験手法

ELECTRON MICROSCOPY (2.9 Å)