Division of Clinical and Molecular Allergology, Research Center Borstel, Priority Research Area Asthma and Allergy, Airway Research Center North (ARCN), German Center for Lung Research (DZL), Borstel, Germany.
Core Facility Fluorescence Cytometry, Research Center Borstel, Borstel, Germany.
J Allergy Clin Immunol. 2017 Nov;140(5):1331-1338.e8. doi: 10.1016/j.jaci.2017.02.020. Epub 2017 Mar 22.
Peanut allergy is one of the most common and most severe food allergies in Western countries and its accurate diagnosis to prevent potential life-threatening allergic reactions is crucial. However, aqueous extracts used for routine diagnostic measurements are devoid of lipophilic allergens such as oleosins. We have recently succeeded in the isolation and purification of these unique proteins, and the present study evaluates their allergenic potential and clinical relevance.
We sought to assess allergenicity and sensitization prevalence of oleosins obtained from both raw and in-shell roasted peanuts. In addition, we tested the utilization of natural and recombinant oleosins for allergy diagnostic purposes.
Oleosin sensitization, prevalence, and impact of thermal processing were analyzed by immunoblot with sera from 52 peanut-allergic individuals displaying different clinical phenotypes. The application of natural and recombinant oleosins for allergy diagnostics was investigated by basophil activation test (BAT). IgE-binding epitopes were identified by oligopeptide microarray.
Sensitization to oleosins was observed exclusively in peanut-allergic subjects suffering from severe systemic reactions. IgE-binding capacity of oleosins derived from in-shell roasted peanuts was increased as shown by immunoblot analysis and BAT. Both natural and recombinant molecules can be used to identify oleosin-sensitized patients by BAT. A linear epitope of Ara h 15 was determined that displays high similarity to other seed-derived oleosins.
Oleosins are clinically relevant peanut allergens and most likely associated with severe allergic symptoms. In-shell roasting increases their allergenicity, which is consistent with the observation that most allergic reactions are in connection with roasted peanuts.
花生过敏是西方国家最常见和最严重的食物过敏之一，准确诊断以预防潜在的危及生命的过敏反应至关重要。然而，用于常规诊断测量的水性提取物缺乏亲脂性过敏原，如油体蛋白。我们最近成功地分离和纯化了这些独特的蛋白质，本研究评估了它们的变应原性和临床相关性。
我们旨在评估从生花生和带壳烤花生中获得的油体蛋白的变应原性和致敏流行率。此外，我们还测试了天然和重组油体蛋白在过敏诊断中的应用。
通过免疫印迹法分析 52 名具有不同临床表型的花生过敏个体的血清，分析油体蛋白的致敏性、流行率和热加工的影响。通过嗜碱性粒细胞活化试验（BAT）研究天然和重组油体蛋白在过敏诊断中的应用。通过寡肽微阵列鉴定 IgE 结合表位。
仅在患有严重全身性反应的花生过敏患者中观察到对油体蛋白的致敏。免疫印迹分析和 BAT 显示，来自带壳烤花生的油体蛋白的 IgE 结合能力增加。天然和重组分子都可用于通过 BAT 识别油体蛋白致敏患者。确定了 Ara h 15 的线性表位，该表位与其他种子衍生的油体蛋白具有高度相似性。
油体蛋白是临床相关的花生过敏原，很可能与严重过敏症状有关。带壳烘烤会增加其变应原性，这与大多数过敏反应与烤花生有关的观察结果一致。
