Global Research, ALK-Abelló A/S, Hørsholm, Denmark.
Biostructural Research, Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.
Allergy. 2017 Apr;72(4):665-670. doi: 10.1111/all.13111. Epub 2017 Jan 19.
The Blomia tropicalis (Blo t) mite species is considered a storage mite in temperate climate zones and an important source of indoor allergens causing allergic asthma and rhinitis in tropical and subtropical regions. Here, we report the crystal structure of one of the allergens from Blo t, recombinant proBlo t 1 (rproBlo t 1), determined at 2.1 Å resolution. Overall, the fold of rproBlo t 1 is characteristic for the pro-form of cysteine proteases from the C1A class. Structural comparison of experimentally mapped Der f 1/Der p1 IgG epitopes to the same surface patch on Blo t 1, as well as of sequence identity of surface-exposed residues, suggests limited cross-reactivity between these allergens and Blo t 1. This is in agreement with ELISA inhibition results showing that, although cross-reactive human IgE epitopes exist, there are unique IgE epitopes for both Blo t 1 and Der p 1.
布氏嗜鳞螨（Blo t）被认为是温带气候带中的贮藏性螨，也是热带和亚热带地区引起过敏哮喘和鼻炎的重要室内过敏原来源。在这里，我们报告了布氏嗜鳞螨过敏原之一重组 proBlo t 1（rproBlo t 1）的晶体结构，其分辨率为 2.1 Å。总体而言，rproBlo t 1 的折叠结构特征为 C1A 类半胱氨酸蛋白酶的前体形式。实验映射的 Der f 1/Der p1 IgG 表位与 Blo t 1 同一表面斑块的结构比较，以及表面暴露残基的序列同一性，表明这些过敏原与 Blo t 1 之间的交叉反应有限。这与 ELISA 抑制结果一致，表明虽然存在交叉反应性人 IgE 表位，但 Blo t 1 和 Der p 1 都具有独特的 IgE 表位。
