Tretter V, Altmann F, Kubelka V, März L, Becker W M
Institut für Chemie, Universität für Bodenkultur, Wien, Osterreich.
Int Arch Allergy Immunol. 1993;102(3):259-66. doi: 10.1159/000236534.
The reactivity of sera from honeybee venom allergic patients with the N-glycan of phospholipase A2 was investigated using neoglycoproteins with an enzyme-linked immunosorbent assay. Of 122 sera with appreciable levels of IgE antibodies directed against bee venom as measured by radioallergosorbent test, 34 sera exhibited significant amounts of glycan-reactive IgE. These sera cross-reacted with the N-glycan from the plant glycoprotein bromelain. The interaction of IgE with the N-glycan from phospholipase could be inhibited with glycopeptides from bromelain which shares the alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine with bee venom phospholipase. Since defucosylated bromelain glycopeptides or glycopeptides containing a Man3GlcNAc2 oligosaccharide were not recognized by most of these sera, we conclude that alpha 1,3-fucosylation of the innermost N-acetylglucosamine residue of N-glycoproteins forms an IgE-reactive determinant. This structural element is frequent in glycoproteins from plants, and it occurs also in insects. It is suspected to be one of the major causes of the broad allergenic cross-reactivity among various allergens from insects and plants.
利用新糖蛋白和酶联免疫吸附测定法，研究了蜜蜂毒液过敏患者血清与磷脂酶A2的N -聚糖的反应性。通过放射变应原吸附试验测定，在122份对蜂毒有明显水平IgE抗体的血清中，有34份血清表现出大量的聚糖反应性IgE。这些血清与植物糖蛋白菠萝蛋白酶的N -聚糖发生交叉反应。IgE与磷脂酶N -聚糖的相互作用可被菠萝蛋白酶的糖肽抑制，该糖肽与蜂毒磷脂酶共享天冬酰胺结合的N -乙酰葡糖胺的α1,3 -岩藻糖基化。由于去岩藻糖基化的菠萝蛋白酶糖肽或含有Man3GlcNAc2寡糖的糖肽未被大多数这些血清识别，我们得出结论，N -糖蛋白最内层N -乙酰葡糖胺残基的α1,3 -岩藻糖基化形成了一个IgE反应性决定簇。这种结构元件在植物糖蛋白中很常见，在昆虫中也存在。它被怀疑是昆虫和植物各种过敏原之间广泛的过敏交叉反应的主要原因之一。
