4UNZ

Structure of the A_Equine_Newmarket_2_93 H3 haemagglutinin in complex with 6SO4-Sialyl Lewis X

4UNZ の概要

• エントリーDOI: 10.2210/pdb4unz/pdb
• 関連するPDBエントリー: 4UNW 4UNX 4UNY 4UO0 4UO1 4UO2 4UO3 4UO4 4UO5 4UO6 4UO7 4UO8 4UO9 4UOA
• 分子名称: HAY SUBUNIT OF HAEMAGGLUTININ, 2-acetamido-2-deoxy-beta-D-glucopyranose, H3 HAEMAGGLUTININ HA2 CHAIN, ... (11 entities in total)
• 機能のキーワード: viral protein, influenza
• 由来する生物種: INFLUENZA A VIRUS (A/EQ/NEWMARKET/93/(H3N8)); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 180218.33

構造登録者

Vachieri, S.G.,Collins, P.J.,Haire, L.F.,Ogrodowicz, R.W.,Martin, S.R.,Walker, P.A.,Xiong, X.,Gamblin, S.J.,Skehel, J.J. (登録日: 2014-05-31, 公開日: 2014-07-23, 最終更新日: 2024-01-10)

主引用文献

Collins, P.J.,Vachieri, S.G.,Haire, L.F.,Ogrodowicz, R.W.,Martin, S.R.,Walker, P.A.,Xiong, X.,Gamblin, S.J.,Skehel, J.J.
Recent Evolution of Equine Influenza and the Origin of Canine Influenza.
Proc.Natl.Acad.Sci.USA, 111:11175-, 2014

PubMed Abstract: In 2004 an hemagglutinin 3 neuraminidase 8 (H3N8) equine influenza virus was transmitted from horses to dogs in Florida and subsequently spread throughout the United States and to Europe. To understand the molecular basis of changes in the antigenicity of H3 hemagglutinins (HAs) that have occurred during virus evolution in horses, and to investigate the role of HA in the equine to canine cross-species transfer, we used X-ray crystallography to determine the structures of the HAs from two antigenically distinct equine viruses and from a canine virus. Structurally all three are very similar with the majority of amino acid sequence differences between the two equine HAs located on the virus membrane-distal molecular surface. HAs of canine viruses are distinct in containing a Trp-222 → Leu substitution in the receptor binding site that influences specificity for receptor analogs. In the fusion subdomain of canine and recent equine virus HAs a unique difference is observed by comparison with all other HAs examined to date. Analyses of site-specific mutant HAs indicate that a single amino acid substitution, Thr-30 → Ser, influences interactions between N-terminal and C-terminal regions of the subdomain that are important in the structural changes required for membrane fusion activity. Both structural modifications may have facilitated the transmission of H3N8 influenza from horses to dogs.

PubMed: 25024224
DOI: 10.1073/PNAS.1406606111

実験手法

X-RAY DIFFRACTION (2.9 Å)