Vieths S, Jankiewicz A, Wüthrich B, Baltes W
Institute of Food Chemistry, Technische Universität Berlin, Germany.
Ann Allergy Asthma Immunol. 1995 Jul;75(1):48-55.
The purpose of this study was to characterize the IgE binding components of celery root by immunoblot analysis and to investigate the cross-reactive nature of the allergens.
Sensitization to celery is very common in patients hypersensitive to mugwort pollen and birch pollen, and is due to cross-reactions of allergen-specific IgE antibodies. Recently, the pan-allergen profilin has been identified as an important cross-reactive allergen in celery, birch pollen and mugwort pollen. Very few data, however, on additional celery allergens are available.
Sera of 38 patients with an isolated or combined sensitization to birch pollen, mugwort pollen, and celery were investigated by immunoblot and immunoblot inhibition techniques using celery extract and purified Bet v I, the major allergen from birch pollen. The selection of sera was based on serologic sensitization, independent of clinical manifestations. Celery profilin was affinity isolated and analyzed by immunoblotting with patients' sera as well as with rabbit polyclonal antiserum raised against celery profilin.
Only weak IgE binding occurred on celery immunoblots in the patient groups with a negative RAST to celery. Sera of 6/8 patients with a birch pollen/celery sensitization recognized a 16-kDa celery allergen that cross-reacted with Bet v I in immunoblot inhibition experiments. In the mugwort pollen/celery and birch pollen/mugwort pollen/celery patient groups, the sera of 6/16 patients contained IgE that bound to a 15 to 16-kDa double band identified as celery profilin. Furthermore, three sera of the birch pollen/mugwort pollen/celery group appeared to contain IgE antibodies against carbohydrate determinants.
The 16-kDa Bet v I-related celery protein appears to be an important allergen for patients sensitized to birch pollen and celery. In contrast IgE binding to celery profilin appears to be more important in patients with an additional sensitization to mugwort pollen.
本研究旨在通过免疫印迹分析来鉴定芹菜根中的IgE结合成分,并研究过敏原的交叉反应特性。
对艾蒿花粉和桦树花粉过敏的患者中,对芹菜过敏很常见,这是由于过敏原特异性IgE抗体的交叉反应所致。最近,泛过敏原肌动蛋白结合蛋白已被鉴定为芹菜、桦树花粉和艾蒿花粉中的一种重要交叉反应性过敏原。然而,关于其他芹菜过敏原的数据非常少。
采用芹菜提取物和纯化的桦树花粉主要过敏原Bet v I,通过免疫印迹和免疫印迹抑制技术,对38例对桦树花粉、艾蒿花粉和芹菜单一或联合致敏的患者血清进行研究。血清的选择基于血清学致敏情况,与临床表现无关。亲和分离芹菜肌动蛋白结合蛋白,并用患者血清以及针对芹菜肌动蛋白结合蛋白产生的兔多克隆抗血清进行免疫印迹分析。
对芹菜RAST阴性的患者组中,芹菜免疫印迹上仅出现微弱的IgE结合。6/8例桦树花粉/芹菜致敏患者的血清识别出一种16 kDa的芹菜过敏原,该过敏原在免疫印迹抑制实验中与Bet v I发生交叉反应。在艾蒿花粉/芹菜和桦树花粉/艾蒿花粉/芹菜患者组中,6/16例患者的血清中含有与鉴定为芹菜肌动蛋白结合蛋白的15至16 kDa双条带结合的IgE。此外,桦树花粉/艾蒿花粉/芹菜组的三份血清似乎含有针对碳水化合物决定簇的IgE抗体。
16 kDa的与Bet v I相关的芹菜蛋白似乎是对桦树花粉和芹菜致敏患者的一种重要过敏原。相比之下,对艾蒿花粉额外致敏患者中,IgE与芹菜肌动蛋白结合蛋白的结合似乎更为重要。