Division of Allergy and Clinical Immunology, Department of Medicine, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Immunol Res. 2013 Mar;55(1-3):125-34. doi: 10.1007/s12026-012-8355-x.
Food allergy has become a major public health concern in westernized countries, and allergic reactions to peanuts are particularly common and severe. Allergens are defined as antigens that elicit an IgE response, and most allergenic materials (e.g., pollens, danders, and foods) contain multiple allergenic proteins. This has led to the concept that there are "major" allergens and allergens of less importance. "Major allergens" have been defined as allergens that bind a large amount of IgE from the majority of patients and have biologic activity. However, the ability of an allergen to cross-link complexes of IgE and its high-affinity receptor FcεRI (IgE/FcεRI), which we have termed its allergic effector activity, does not correlate well with assays of IgE binding. To identify the proteins that are the most active allergens in peanuts, we and others have employed in vitro model assays of allergen-mediated cross-linking of IgE/FcεRI complexes and have demonstrated that the most potent allergens are not necessarily those that bind the most IgE. The importance of a specific allergen can be determined by measuring the allergic effector activity of that allergen following purification under non-denaturing conditions and by specifically removing the allergen from a complex allergenic extract either by chromatography or by specific immunodepletion. In our studies of peanut allergens, our laboratory has found that two related allergens, Ara h 2 and Ara h 6, together account for the majority of the effector activity in a crude peanut extract. Furthermore, murine studies demonstrated that Ara h 2 and Ara h 6 are not only the major elicitors of anaphylaxis in this system, but also can effectively desensitize peanut-allergic mice. As a result of these observations, we propose that the definition of a major allergen should be based on the potency of that allergen in assays of allergic effector activity and demonstration that removal of that allergen from an extract results in loss of potency. Using these criteria, Ara h 2 and Ara h 6 are the major peanut allergens.
食物过敏已成为西方国家主要的公共卫生问题,而花生过敏尤其常见且严重。过敏原被定义为能引起 IgE 反应的抗原,大多数过敏原物质(如花粉、皮屑和食物)都含有多种过敏原蛋白。这就产生了“主要”过敏原和不太重要的过敏原的概念。“主要过敏原”被定义为能与大多数患者的大量 IgE 结合并具有生物活性的过敏原。然而,过敏原与 IgE 及其高亲和力受体 FcεRI(IgE/FcεRI)交联复合物的能力及其过敏效应活性与其 IgE 结合测定并不相符。为了确定花生中最活跃的过敏原蛋白,我们和其他人采用了体外模型测定过敏原介导的 IgE/FcεRI 复合物交联,并证明最有效的过敏原不一定是与最多 IgE 结合的过敏原。特定过敏原的重要性可以通过在非变性条件下纯化后测量该过敏原的过敏效应活性,并通过色谱或特异性免疫耗竭从复杂的变应原提取物中特异性去除过敏原来确定。在我们对花生过敏原的研究中,我们实验室发现两种相关的过敏原 Ara h 2 和 Ara h 6 共同构成了粗花生提取物中大多数效应活性的来源。此外,鼠类研究表明,Ara h 2 和 Ara h 6 不仅是该系统中过敏反应的主要引发剂,而且还可以有效地使花生过敏的小鼠脱敏。基于这些观察结果,我们提出主要过敏原的定义应基于该过敏原在过敏效应活性测定中的效力以及从提取物中去除该过敏原会导致效力丧失的证据。使用这些标准,Ara h 2 和 Ara h 6 是主要的花生过敏原。