ROLE OF FOOD HYPERSENSITIVITY IN ATOPIC DERMATITIS

我们以前证明卵类粘蛋白，Gal d 1， 鸡蛋中的过敏原 卵类粘蛋白是一种高度糖基化的蛋白质 由排列在3个串联结构域中的186个氨基酸组成[Gald1.1， 1.2，1.3]，每个长度约60个氨基酸。 本研究的目的 是为了评估卵类粘蛋白的致敏性。 我们分离出 通过酶消化和色谱法测定3个卵类粘蛋白结构域 洁净. 45例鸡蛋过敏性异位性皮炎患者血清分析 通过ELISA分析以确定B细胞结构域特异性; 通过抑制ELISA分析鸡蛋过敏患者， 烷基化、氧化和去糖基化卵类粘蛋白，以评估 线性和构象结构以及碳水化合物对B重要性 细胞表位 13例鸡蛋过敏患者外周血T细胞的检测 用于评估T-显性结构域和对还原和还原的反应性， 氧化卵类粘蛋白 几乎所有的患者都有IgE抗体的3个领域，虽然有 IgE活性显著高于Gal d 1.2 [卵类粘蛋白百分比， 特异性IgE;中位数：Gal d 1.2：40%; Gal d 1.1：23%; Gal d 1.3：26%]。 患者IgG抗体的效价与所有3个结构域相当。 IgE 抗体与还原卵类粘蛋白的结合和IgG与氧化卵类粘蛋白的结合 与天然卵类粘蛋白相比，卵类粘蛋白显著减少[28%， 69%）。33个外周血T细胞中有21个对 Gal d 1.3，33例中的18例为Gal d 1.2，33例中的18例为Gal d 1.1。 T细胞 体外增殖对还原型和氧化型卵类粘蛋白的影响 明显高于天然蛋白质。 这些结果表明，T细胞和B细胞之间存在二分法， 优势，以及IgE和IgG表位的差异。 此外，结果 表明构象B细胞表位起更重要作用 卵类粘蛋白过敏原在某些患者，特别是那些 “短暂的”鸡蛋过敏症比以前认识到， 碳水化合物部分对变应原性的影响较小。

We previously demonstrated that ovomucoid, Gal d 1, is the dominant allergen in hen's egg. Ovomucoid is a highly glycosylated protein comprised of 186 amino acids arranged in 3 tandem domains [Gal d 1.1, 1.2, 1.3], each about 60 amino acids in length. The purpose of this study was to evaluate the allergenic properties of ovomucoid. We isolated the 3 ovomucoid domains by enzymatic digestion and chromatographic purification. Sera from 45 egg allergic patients with atoppic dermatitis were anlyzed by ELISA to determine B cell domain specificity; sera from egg allergic patients were analyzed by inhibition-ELISA to reduce and alkylated, oxidized, and deglycosylated ovomucoid in order to evaluate the importance of linear and conformational structures, and carbohydrate to B cell epitopes. Peripheral blood T cells from 13 egg allergic patients were used to evaluate T-dominant domains and reactivity to reduced and oxidized ovomucoid. Virtually all patients had IgE antibodies to the 3 domains, although there was significalty more IgE activity to Gal d 1.2 [percentage of ovomucoid- specific IgE; median: Gal d 1.2: 40%; Gal d 1.1:23%; Gal d 1.3 26%]. Quantities of patient IgG antibody was comparable to all 3 domains. IgE antibody binding to reduced ovomucoid and IgG binding to oxidized ovomucoid were significantly reduced compared to native ovomucoid [28% and 69%, respectively]. Twenty-one of 33 peripheral blood T cells reacted to Gal d 1.3, 18 of 33 to Gal d 1.2, and 18 of 33 to Gal d 1.1. T cell proliferation in vitro to reduced and oxidized ovomucoid were significantly greater than to the native protein. These results indicate a dichotomy between T cell and B cell comain dominance, and differences in IgE and IgG epitopes. Furthermore results suggest that conformational B cell epitopes play a more significant role in ovomucoid allergenicity in some patients, especially those with "transient" egg hypersensitivity than previously appreciated, and that carbohydrate moieties have a minor effect on allergenicity.