5BR3

Crystal structure of hemagglutinin of A/Taiwan/2/2013 (H6N1) in complex with LSTa

5BR3 の概要

• エントリーDOI: 10.2210/pdb5br3/pdb
• 関連するPDBエントリー: 5BNY 5BQY 5BQZ 5BR0 5BR6
• 分子名称: HEMAGGLUTININ HA1 CHAIN, HEMAGGLUTININ HA2 CHAIN, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: influenza, heamgglutinin, viral protein
• 由来する生物種: Influenza A virus; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 118021.22

構造登録者

Ni, F.,Kondrashkina, E.,Wang, Q. (登録日: 2015-05-29, 公開日: 2015-08-12, 最終更新日: 2024-11-20)

主引用文献

Ni, F.,Kondrashkina, E.,Wang, Q.
Structural and Functional Studies of Influenza Virus A/H6 Hemagglutinin.
Plos One, 7:e0134576-e0134576, 2015

PubMed Abstract: In June 2013, the first human infection by avian influenza A(H6N1) virus was reported in Taiwan. This incident raised the concern for possible human epidemics and pandemics from H6 viruses. In this study, we performed structural and functional investigation on the hemagglutinin (HA) proteins of the human-infecting A/Taiwan/2/2013(H6N1) (TW H6) virus and an avian A/chicken/Guangdong/S1311/2010(H6N6) (GD H6) virus that transmitted efficiently in guinea pigs. Our results revealed that in the presence of HA1 Q226, the triad of HA1 S137, E190 and G228 in GD H6 HA allows the binding to both avian- and human-like receptors with a slight preference for avian receptors. Its conservation among the majority of H6 HAs provides an explanation for the broader host range of this subtype. Furthermore, the triad of N137, V190 and S228 in TW H6 HA may alleviate the requirement for a hydrophobic residue at HA1 226 of H2 and H3 HAs when binding to human-like receptors. Consequently, TW H6 HA has a slight preference for human receptors, thus may represent an intermediate towards a complete human adaptation. Importantly, the triad observed in TW H6 HA is detected in 74% H6 viruses isolated from Taiwan in the past 14 years, suggesting an elevated threat of H6 viruses from this region to human health. The novel roles of the triad at HA1 137, 190 and 228 of H6 HA in binding to receptors revealed here may also be used by other HA subtypes to achieve human adaptation, which needs to be further tested in laboratory and closely monitored in field surveillance.

PubMed: 26226046
DOI: 10.1371/journal.pone.0134576

実験手法

X-RAY DIFFRACTION (2.55 Å)