5XL4

The structure of hemagglutinin from an avian-origin H4N6 influenza virus in complex with human receptor analog Lstc

5XL4 の概要

• エントリーDOI: 10.2210/pdb5xl4/pdb
• 分子名称: Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose, N-acetyl-alpha-neuraminic acid, ... (5 entities in total)
• 機能のキーワード: h4 hemagglutinin, influenza virus, receptor binding, viral protein
• 由来する生物種: Influenza A virus (strain A/Duck/Czechoslovakia/1956 H4N6); 詳細
• 細胞内の位置: Host apical cell membrane ; Single-pass type I membrane protein : A3KF09 A3KF09
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114121.08

構造登録者

Song, H.,Qi, J.,Gao, G.F. (登録日: 2017-05-10, 公開日: 2017-08-02, 最終更新日: 2024-10-09)

主引用文献

Song, H.,Qi, J.,Xiao, H.,Bi, Y.,Zhang, W.,Xu, Y.,Wang, F.,Shi, Y.,Gao, G.F.
Avian-to-Human Receptor-Binding Adaptation by Influenza A Virus Hemagglutinin H4
Cell Rep, 20:1201-1214, 2017

PubMed Abstract: Low-pathogenicity avian influenza viruses (LPAIVs) have caused a global concern to public health since the first novel LPAIV H7N9 outbreak occurred. The receptor-binding properties of the viral hemagglutinin are one key factor for efficient transmission and infection in humans. Recent evidence shows that H4 subtype viruses have been widely circulating in domestic poultry and human asymptomatic infections might have occurred. Here, we evaluated the receptor-binding properties of two representative isolates, avian H4N6 (containing Q226 and G228) and swine H4N6 (containing L226 and S228), and found that the avian isolate preferentially binds to avian receptors, whereas the swine isolate preferentially binds to human receptors. The Q226L and G228S substitutions are pivotal for the receptor-binding switch, which resulted in similar human receptor-binding features to the pandemic H2 and H3, implying that H4 has the potential to cause human infections. This early-warning study calls for future extensive surveillance.

PubMed: 28768203
DOI: 10.1016/j.celrep.2017.07.028

実験手法

X-RAY DIFFRACTION (2.102 Å)