Eigenmann P A, Burks A W, Bannon G A, Sampson H A
Johns Hopkins University School of Medicine, Baltimore, MD, USA.
J Allergy Clin Immunol. 1996 Nov;98(5 Pt 1):969-78. doi: 10.1016/s0091-6749(96)80014-5.
Soybean and peanut are members of the legume family and share several common antigenic fractions. Patients allergic to one of these foods have serum IgE antibodies that immunologically cross-react with other legumes. Nevertheless, ingestion of other legumes generally does not induce an allergic reaction, suggesting that cross-reacting antibodies are not clinically relevant.
This study was designed to identify unique peanut or soybean antigenic fractions, with sera adsorbed to remove cross-reacting antibodies, thus resulting in sera with IgE antibodies unique to either soy or peanut.
Cross-reacting antibodies to soy were removed from the sera of two patients allergic to peanut and soy and three patients allergic to peanut by soy-affinity chromatography. Cross-reacting antibodies to peanut were adsorbed from the sera of a patient allergic to peanut and soy and a patient allergic to peanut by peanut-affinity chromatography. Adequate removal of cross-reacting antibodies was verified by ELISA after each adsorption step. Unadsorbed sera and sera adsorbed to remove cross-reacting antibodies (either to soy or to peanut) were assayed for specific IgE binding to peanut or soy immunoblots.
Unique peanut-specific IgE antibodies (i.e., soy antibody-adsorbed) were found to bind to peanut fractions at 46, 29, 25, 19, 17, 14, and 5 kd on immunoblots of whole peanut protein. Similarly, unique soy-specific IgE (i.e., peanut antibody-adsorbed) were found to bind a fraction at 46 kd, and to a lesser extent, to a fraction at 21 kd on immunoblots of whole soy protein. The 73% reduction of IgE antibody binding to peanut by ELISA after adsorption of cross-reacting antibodies indicates extensive cross-reactivity between soy and peanut antigens.
Antigen-affinity chromatography is an effective method for removal of cross-reacting antibodies. We identified IgE antibody binding (with sera where cross-reacting antibodies were removed) to several unique antigenic fractions of peanut and soy. Further studies will determine the clinical significance of these fractions in IgE-mediated food hypersensitivity reactions.
大豆和花生属于豆科植物,具有几种共同的抗原成分。对其中一种食物过敏的患者血清中存在免疫球蛋白E(IgE)抗体,这些抗体可与其他豆类发生免疫交叉反应。然而,摄入其他豆类通常不会引发过敏反应,这表明交叉反应抗体在临床上并无相关性。
本研究旨在识别独特的花生或大豆抗原成分,通过吸附血清去除交叉反应抗体,从而获得仅对大豆或花生具有特异性IgE抗体的血清。
通过大豆亲和层析从两名对花生和大豆过敏的患者以及三名对花生过敏的患者血清中去除针对大豆的交叉反应抗体。通过花生亲和层析从一名对花生和大豆过敏的患者以及一名对花生过敏的患者血清中吸附针对花生的交叉反应抗体。每次吸附步骤后通过酶联免疫吸附测定(ELISA)验证交叉反应抗体是否被充分去除。对未吸附的血清以及吸附去除交叉反应抗体(针对大豆或花生)后的血清进行检测,以确定其与花生或大豆免疫印迹的特异性IgE结合情况。
在全花生蛋白免疫印迹上,发现独特的花生特异性IgE抗体(即吸附了大豆抗体的血清)可与46、29、25、19、17、14和5千道尔顿(kd)的花生成分结合。同样,在全大豆蛋白免疫印迹上,发现独特的大豆特异性IgE(即吸附了花生抗体的血清)可与46 kd的成分结合,并在较小程度上与21 kd的成分结合。吸附交叉反应抗体后,ELISA检测显示IgE抗体与花生的结合减少了73%,这表明大豆和花生抗原之间存在广泛的交叉反应性。
抗原亲和层析是去除交叉反应抗体的有效方法。我们确定了(去除交叉反应抗体后的血清中)IgE抗体与花生和大豆的几种独特抗原成分的结合情况。进一步研究将确定这些成分在IgE介导的食物过敏反应中的临床意义。