Mattison Christopher P, Desormeaux Wendy A, Wasserman Richard L, Yoshioka-Tarver Megumi, Condon Brian, Grimm Casey C
Southern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, New Orleans, Louisiana 70124, United States.
J Agric Food Chem. 2014 Jul 16;62(28):6746-55. doi: 10.1021/jf501117p. Epub 2014 Jul 1.
Cashew nut and other nut allergies can result in serious and sometimes life-threatening reactions. Linear and conformational epitopes within food allergens are important for immunoglobulin E (IgE) binding. Methods that disrupt allergen structure can lower IgE binding and lessen the likelihood of food allergy reactions. Previous structural and biochemical data have indicated that 2S albumins from tree nuts and peanuts are potent allergens, and that their structures are sensitive to strong reducing agents such as dithiothreitol. This study demonstrates that the generally regarded as safe (GRAS) compound sodium sulfite effectively disrupted the structure of the cashew 2S albumin, Ana o 3, in a temperature-dependent manner. This study also showed that sulfite is effective at disrupting the disulfide bond within the cashew legumin, Ana o 2. Immunoblotting and ELISA demonstrated that the binding of cashew proteins by rabbit IgG or IgE from cashew-allergic patients was markedly lowered following treatment with sodium sulfite and heating. The results indicate that incorporation of sodium sulfite, or other food grade reagents with similar redox potential, may be useful processing methods to lower or eliminate IgE binding to food allergens.
腰果和其他坚果过敏可能会导致严重的、有时甚至危及生命的反应。食物过敏原中的线性和构象表位对于免疫球蛋白E（IgE）结合很重要。破坏过敏原结构的方法可以降低IgE结合，并减少食物过敏反应的可能性。先前的结构和生化数据表明，来自坚果和花生的2S白蛋白是强效过敏原，并且它们的结构对强还原剂如二硫苏糖醇敏感。本研究表明，一般认为安全（GRAS）的化合物亚硫酸钠以温度依赖的方式有效地破坏了腰果2S白蛋白Ana o 3的结构。本研究还表明，亚硫酸盐可有效破坏腰果豆球蛋白Ana o 2中的二硫键。免疫印迹和酶联免疫吸附测定表明，用亚硫酸钠处理并加热后，来自腰果过敏患者的兔IgG或IgE与腰果蛋白的结合显著降低。结果表明，加入亚硫酸钠或其他具有相似氧化还原电位的食品级试剂，可能是降低或消除IgE与食物过敏原结合的有用加工方法。
