Crystal structure of peanut (Arachis hypogaea) allergen Ara h 5.
Crystal structure of peanut (Arachis hypogaea) allergen Ara h 5.
复制标题
花生（Arachishypogaea）过敏原 Ara h 5 的晶体结构。
DOI：
10.1021/jf303861p
复制
发表时间：
2013
影响因子：
6.1
通讯作者：
Zhang,Yuzhu
中科院分区：
文献类型：
--
作者：
Wang,Yang;Fu,Tong-Jen;Howard,Andrew;Kothary,MahendraH;McHugh,TaraH;Zhang,Yuzhu
已知来自许多物种的profilin是过敏原，包括食物过敏原，例如花生（Arachis hypogaea）过敏原Ara h 5，和花粉过敏原，例如桦树过敏原Bet v 2。花粉过敏的患者也会对花生产生交叉反应。过敏原的结构表征将使人们更好地了解食物过敏原的过敏原性及其交叉反应性。大多数已知的食物过敏原的三维结构仍有待阐明。在这里，我们报告的第一个晶体学研究的食物过敏原的profilin家庭。对花生过敏原Ara h 5进行了结构测定，最终精制结构的分辨率为1. 1 μ m。结构比对显示Ara h 5与Bet v 2的相似性大于与Hev B 8的相似性，尽管序列比对表明Ara h 5与Hev B 8的相似性大于与Bet v 2的相似性，这表明基于同源性模型的免疫球蛋白E表位预测需要谨慎解释。
Profilins from numerous species are known to be allergens, including food allergens, such as peanut (Arachis hypogaea) allergen Ara h 5, and pollen allergens, such as birch allergen Bet v 2. Patients with pollen allergy can also cross-react to peanut. Structural characterization of allergens will allow a better understanding of the allergenicity of food allergens and their cross-reactivities. The three-dimensional structures of most known food allergens remain to be elucidated. Here, we report the first crystallographic study of a food allergen in the profilin family. The structure of peanut allergen Ara h 5 was determined, and the resolution of the final refined structure was 1.1 Å. Structure alignment revealed that Ara h 5 is more similar to Bet v 2 than to Hev b 8, although sequence alignment suggested that Ara h 5 is more closely related to Hev b 8 than to Bet v 2, indicating that homology-model-based prediction of immunoglobulin E epitopes needs to be interpreted with caution.