de Jong E C, Van Zijverden M, Spanhaak S, Koppelman S J, Pellegrom H, Penninks A H
TNO Nutrition and Food Research Institute, Immunotoxicology group, Zeist, The Netherlands.
Clin Exp Allergy. 1998 Jun;28(6):743-51. doi: 10.1046/j.1365-2222.1998.00301.x.
Peanuts are a major cause of food allergies both in children as in adults which can induce an anaphylactic shock. The identification and characterization of peanut allergens could lead to more insight into the mechanism and contribute to the improvement of diagnostic tests and treatment for peanut allergy.
In the present study, the peanut protein-specific immunoglobulin concentrations as well as their recognition of the various peanut proteins or protein subunits was determined in the plasma of peanut-allergic (PA) and non-allergic (NA) individuals. Moreover, two peanut allergens were characterized in more detail to confirm them as the earlier described Ara h1 and Ara h2.
The presence of Ig-binding sites in peanut proteins was studied by immunoblotting assays whereas the concentrations of peanut-specific Ig was determined by ELISA.
Peanut proteins were found to contain multiple binding sites for immunoglobulins. Of these proteins, six were recognized by peanut-specific IgE present in more than 50% of the plasma samples of the PA group. Their molecular weights were approximately 44, 40, 33, 21, 20 and 18 kDa. The last three protein bands were recognized by peanut-specific IgE present in more than 70% of the PA plasma samples and were thought to contain Ara h2. This allergen as well as another protein that was thought to be Ara h1, which was not recognized by the majority of the patients' IgE-containing plasma samples, were isolated and the N terminal amino acid sequence was determined. Peanut protein-specific IgA, IgM, IgG and IgG-subclasses showed a more diverse recognition pattern of peanut protein in the PA group compared to the NA group. No differences were found in the plasma concentrations of peanut protein-specific immunoglobulins of the various classes between the PA and NA group.
From the present study, we conclude that peanuts contain multiple allergens, of which six can be described as major allergens, Ara h2 included. In our population Ara h1 is not a major allergen. The recognition of peanut proteins by immunoglobulins is more diverse in PA individuals compared with NA individuals which, however, is not substantiated in the concentrations of peanut-specific immunoglobulins in plasma, other than IgE.
花生是儿童和成人食物过敏的主要原因，可引发过敏性休克。花生过敏原的鉴定和特性分析有助于更深入了解其机制，并有助于改进花生过敏的诊断测试和治疗方法。
在本研究中，测定了花生过敏（PA）和非过敏（NA）个体血浆中花生蛋白特异性免疫球蛋白浓度及其对各种花生蛋白或蛋白亚基的识别情况。此外，对两种花生过敏原进行了更详细的特性分析，以确认它们为先前描述的Ara h1和Ara h2。
通过免疫印迹分析研究花生蛋白中Ig结合位点的存在情况，而花生特异性Ig的浓度则通过ELISA测定。
发现花生蛋白含有多个免疫球蛋白结合位点。在这些蛋白中，六种被PA组超过50%的血浆样本中的花生特异性IgE识别。它们的分子量约为44、40、33、21、20和18 kDa。最后三条蛋白带被PA血浆样本中超过70%的花生特异性IgE识别，被认为含有Ara h2。分离出这种过敏原以及另一种被认为是Ara h1的蛋白（大多数含患者IgE的血浆样本未识别该蛋白），并测定了其N端氨基酸序列。与NA组相比，PA组中花生蛋白特异性IgA、IgM、IgG和IgG亚类对花生蛋白的识别模式更为多样。PA组和NA组之间不同类别的花生蛋白特异性免疫球蛋白血浆浓度未发现差异。
从本研究中，我们得出结论，花生含有多种过敏原，其中六种可被描述为主要过敏原，包括Ara h2。在我们的人群中，Ara h1不是主要过敏原。与NA个体相比，PA个体中免疫球蛋白对花生蛋白的识别更为多样，然而，除IgE外，血浆中花生特异性免疫球蛋白的浓度并未证实这一点。
