Obispo T M, Melero J A, Carpizo J A, Carreira J, Lombardero M
Research Department, Alergia e Inmunología Abelló S.A., Madrid, Spain.
Clin Exp Allergy. 1993 Apr;23(4):311-6. doi: 10.1111/j.1365-2222.1993.tb00328.x.
Three major pollen allergens from Fraxinus excelsior, Ligustrum vulgare and Syringa vulgaris belonging to the Oleaceae family were purified. Monoclonal antibodies previously raised against the main allergen of Olea europaea (Ole e I) were used for their purification by affinity chromatography. The three new purified allergens were able to bind human IgE from serum of olive-allergic patients in a way analogous to Ole e I. Crossed radioimmunoelectrophoresis of the four allergens, using anti-olive extract rabbit serum, showed a unique immunoprecipitation arc with the same characteristics. The four purified proteins had similar molecular weights on SDS-PAGE and the N-terminal sequences for the first 20 amino acids were identical. Furthermore, the concentration of the allergens could be determined using a two-side solid phase assay previously developed for the allergen Ole e I. Our results indicate that the four purified proteins share, to a great extent, antigenic and allergenic epitopes leading to cross-reactivities which could cause common clinical manifestations. We propose for the newly purified allergens the nomenclature of Fra e I, Lig v I and Syr v I.
从木犀科的洋白蜡树、女贞和丁香中纯化出了三种主要的花粉过敏原。先前针对油橄榄主要过敏原（Ole e I）产生的单克隆抗体被用于通过亲和色谱法对它们进行纯化。这三种新纯化的过敏原能够以类似于Ole e I的方式结合橄榄过敏患者血清中的人IgE。使用抗橄榄提取物兔血清对这四种过敏原进行交叉放射免疫电泳，显示出具有相同特征的独特免疫沉淀弧。这四种纯化蛋白在SDS-PAGE上具有相似的分子量，并且前20个氨基酸的N端序列相同。此外，使用先前为过敏原Ole e I开发的双侧固相测定法可以测定过敏原的浓度。我们的结果表明，这四种纯化蛋白在很大程度上共享抗原和过敏原表位，导致交叉反应性，可能引起常见的临床表现。我们提议将新纯化的过敏原命名为Fra e I、Lig v I和Syr v I。
