4XQU

Crystal structure of hemagglutinin from Jiangxi-Donghu (2013) H10N8 influenza virus in complex with 3'-SLN

4XQU の概要

• エントリーDOI: 10.2210/pdb4xqu/pdb
• 関連するPDBエントリー: 4XQ5 4XQO
• 関連するBIRD辞書のPRD_ID: PRD_900067
• 分子名称: Hemagglutinin HA1, Hemagglutinin HA2, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: viral protein
• 由来する生物種: Influenza A virus; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 172647.27

構造登録者

Tzarum, N.,Zhang, H.,Zhu, X.,Wilson, I.A. (登録日: 2015-01-20, 公開日: 2015-04-01, 最終更新日: 2024-10-30)

主引用文献

Zhang, H.,de Vries, R.P.,Tzarum, N.,Zhu, X.,Yu, W.,McBride, R.,Paulson, J.C.,Wilson, I.A.
A Human-Infecting H10N8 Influenza Virus Retains a Strong Preference for Avian-type Receptors.
Cell Host Microbe, 17:377-384, 2015

PubMed Abstract: Recent avian-origin H10N8 influenza A viruses that have infected humans pose a potential pandemic threat. Alterations in the viral surface glycoprotein, hemagglutinin (HA), typically are required for influenza A viruses to cross the species barrier for adaptation to a new host, but whether H10N8 contains adaptations supporting human infection remains incompletely understood. We investigated whether H10N8 HA can bind human receptors. Sialoside glycan microarray analysis showed that the H10 HA retains a strong preference for avian receptor analogs and negligible binding to human receptor analogs. Crystal structures of H10 HA with avian and human receptor analogs revealed the basis for preferential recognition of avian-like receptors. Furthermore, introduction of mutations into the H10 receptor-binding site (RBS) known to convert other HA subtypes from avian to human receptor specificity failed to switch preference to human receptors. Collectively, these findings suggest that the current H10N8 human isolates are poorly adapted for efficient human-to-human transmission.

PubMed: 25766296
DOI: 10.1016/j.chom.2015.02.006

実験手法

X-RAY DIFFRACTION (3.25 Å)