Wellhausen A, Schöning B, Petersen A, Vieths S
Institute of Food Chemistry Technische Universität Berlin, FRG.
Z Ernahrungswiss. 1996 Dec;35(4):348-55. doi: 10.1007/BF01610553.
Food allergies in birch pollen allergic patients have been shown to be due to cross-reactivities of specific IgE antibodies which are directed against birch pollen allergens with related proteins in fruit, nuts and vegetables. We identified a new cross-reactive structure of 35 kDa in birch pollen and some plant food extracts by Enzyme Allergosorbent Test (EAST) and immunoblot inhibition studies. The 35 kDa birch pollen protein is a minor allergen to which approximately 10-15% of birch pollen allergic individuals have specific IgE. Our data demonstrate that there is cross-reactivity of this protein with proteins of comparable size from lychee, mango, banana, orange, apple, pear and carrot. While the 35 kDa protein is immunologically independent of the major birch pollen allergen Bet v 1, we also observed IgE binding to a 34 kDa structure which appears to be a Bet v 1 dimer.
桦树花粉过敏患者的食物过敏已被证明是由于特异性IgE抗体的交叉反应性，这些抗体针对桦树花粉过敏原以及水果、坚果和蔬菜中的相关蛋白质。我们通过酶联免疫吸附试验（EAST）和免疫印迹抑制研究，在桦树花粉和一些植物性食物提取物中鉴定出一种新的35 kDa交叉反应结构。35 kDa的桦树花粉蛋白是一种次要过敏原，约10%-15%的桦树花粉过敏个体对其有特异性IgE。我们的数据表明，该蛋白与荔枝、芒果、香蕉、橙子、苹果、梨和胡萝卜中大小相当的蛋白质存在交叉反应。虽然35 kDa蛋白在免疫上独立于主要的桦树花粉过敏原Bet v 1，但我们也观察到IgE与一种34 kDa的结构结合，该结构似乎是Bet v 1二聚体。
