6MLM

H7 HA0 in complex with Fv from H7.5 IgG

6MLM の概要

• エントリーDOI: 10.2210/pdb6mlm/pdb
• EMDBエントリー: 9139
• 分子名称: Hemagglutinin HA1 chain, Hemagglutinin HA2 chain, Heavy chain Fv of H7.5 Fab, ... (5 entities in total)
• 機能のキーワード: hemagglutinin, antibody, fab, h7, ha0, protein complex, viral protein, viral protein-immune system complex, viral protein/immune system
• 由来する生物種: Influenza A virus (A/New York/107/2003(H7N2)); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 327145.45

構造登録者

Pallesen, J.,Turner, H.L.,Ward, A.B. (登録日: 2018-09-27, 公開日: 2019-02-20, 最終更新日: 2024-10-09)

主引用文献

Turner, H.L.,Pallesen, J.,Lang, S.,Bangaru, S.,Urata, S.,Li, S.,Cottrell, C.A.,Bowman, C.A.,Crowe Jr., J.E.,Wilson, I.A.,Ward, A.B.
Potent anti-influenza H7 human monoclonal antibody induces separation of hemagglutinin receptor-binding head domains.
PLoS Biol., 17:e3000139-e3000139, 2019

PubMed Abstract: Seasonal influenza virus infections can cause significant morbidity and mortality, but the threat from the emergence of a new pandemic influenza strain might have potentially even more devastating consequences. As such, there is intense interest in isolating and characterizing potent neutralizing antibodies that target the hemagglutinin (HA) viral surface glycoprotein. Here, we use cryo-electron microscopy (cryoEM) to decipher the mechanism of action of a potent HA head-directed monoclonal antibody (mAb) bound to an influenza H7 HA. The epitope of the antibody is not solvent accessible in the compact, prefusion conformation that typifies all HA structures to date. Instead, the antibody binds between HA head protomers to an epitope that must be partly or transiently exposed in the prefusion conformation. The "breathing" of the HA protomers is implied by the exposure of this epitope, which is consistent with metastability of class I fusion proteins. This structure likely therefore represents an early structural intermediate in the viral fusion process. Understanding the extent of transient exposure of conserved neutralizing epitopes also may lead to new opportunities to combat influenza that have not been appreciated previously.

PubMed: 30716060
DOI: 10.1371/journal.pbio.3000139

実験手法

ELECTRON MICROSCOPY (3.5 Å)