5E32

Crystal structure of H5 hemagglutinin mutant (N224K, Q226L, N158D and L133a deletion) from the influenza virus A/chicken/Vietnam/NCVD-093/2008 (H5N1)

5E32 の概要

• エントリーDOI: 10.2210/pdb5e32/pdb
• 関連するPDBエントリー: 5E2Y 5E2Z 5E30 5E34 5E35
• 分子名称: Hemagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: h5n1 influenza virus, hemagglutinin, receptor binding specificity, transmission, glycan complex, viral protein
• 由来する生物種: Influenza A virus (A/chicken/Vietnam/NCVD-093/2008(H5N1)); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59120.46

構造登録者

Zhu, X.,Wilson, I.A. (登録日: 2015-10-01, 公開日: 2015-12-02, 最終更新日: 2024-10-23)

主引用文献

Zhu, X.,Viswanathan, K.,Raman, R.,Yu, W.,Sasisekharan, R.,Wilson, I.A.
Structural Basis for a Switch in Receptor Binding Specificity of Two H5N1 Hemagglutinin Mutants.
Cell Rep, 13:1683-1691, 2015

PubMed Abstract: Avian H5N1 influenza viruses continue to spread in wild birds and domestic poultry with sporadic infection in humans. Receptor binding specificity changes are a prerequisite for H5N1 viruses and other zoonotic viruses to be transmitted among humans. Previous reported hemagglutinin (HA) mutants from ferret-transmissible H5N1 viruses of A/Vietnam/1203/2004 and A/Indonesia/5/2005 showed slightly increased, but still very weak, binding to human receptors. From mutagenesis and glycan array studies, we previously identified two H5N1 HA mutants that could more effectively switch receptor specificity to human-like α2-6-linked sialosides with avidity comparable to wild-type H5 HA binding to avian-like α2-3-linked sialosides. Here, crystal structures of these two H5 HA mutants free and in complex with human and avian glycan receptor analogs reveal the structural basis for their preferential binding to human receptors. These findings suggest continuous surveillance should be maintained to monitor and assess human-to-human transmission potential of H5N1 viruses.

PubMed: 26586437
DOI: 10.1016/j.celrep.2015.10.027

実験手法

X-RAY DIFFRACTION (2.7 Å)