7UAP

Structure of the SARS-CoV-2 S 6P trimer in complex with the neutralizing antibody Fab fragment, C1520

7UAP の概要

• エントリーDOI: 10.2210/pdb7uap/pdb
• EMDBエントリー: 26429
• 分子名称: Spike glycoprotein, C1520 Fab Heavy Chain, C1520 Fab Light Chain, ... (5 entities in total)
• 機能のキーワード: sars-cov-2, n-terminal domain, ntd, neutralizing antibody, viral protein
• 由来する生物種: Severe acute respiratory syndrome coronavirus 2; 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 575740.04

構造登録者

Barnes, C.O. (登録日: 2022-03-13, 公開日: 2022-04-27, 最終更新日: 2024-11-13)

主引用文献

Wang, Z.,Muecksch, F.,Cho, A.,Gaebler, C.,Hoffmann, H.H.,Ramos, V.,Zong, S.,Cipolla, M.,Johnson, B.,Schmidt, F.,DaSilva, J.,Bednarski, E.,Ben Tanfous, T.,Raspe, R.,Yao, K.,Lee, Y.E.,Chen, T.,Turroja, M.,Milard, K.G.,Dizon, J.,Kaczynska, A.,Gazumyan, A.,Oliveira, T.Y.,Rice, C.M.,Caskey, M.,Bieniasz, P.D.,Hatziioannou, T.,Barnes, C.O.,Nussenzweig, M.C.
Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins.
Immunity, 55:998-1012.e8, 2022

PubMed Abstract: SARS-CoV-2 infection or vaccination produces neutralizing antibody responses that contribute to better clinical outcomes. The receptor-binding domain (RBD) and the N-terminal domain (NTD) of the spike trimer (S) constitute the two major neutralizing targets for antibodies. Here, we use NTD-specific probes to capture anti-NTD memory B cells in a longitudinal cohort of infected individuals, some of whom were vaccinated. We found 6 complementation groups of neutralizing antibodies. 58% targeted epitopes outside the NTD supersite, 58% neutralized either Gamma or Omicron, and 14% were broad neutralizers that also neutralized Omicron. Structural characterization revealed that broadly active antibodies targeted three epitopes outside the NTD supersite including a class that recognized both the NTD and SD2 domain. Rapid recruitment of memory B cells producing these antibodies into the plasma cell compartment upon re-infection likely contributes to the relatively benign course of subsequent infections with SARS-CoV-2 variants, including Omicron.

PubMed: 35447092
DOI: 10.1016/j.immuni.2022.04.003

実験手法

ELECTRON MICROSCOPY (2.8 Å)