Yoshioka Hiroyuki, Ohmoto Tsuyoshi, Urisu Atsuo, Mine Yoshinori, Adachi Taiji
Graduate School of Agricultural and Biological Sciences, Osaka Prefecture University, Gakuen-cho, Sakai, Osaka, Japan.
J Plant Physiol. 2004 Jul;161(7):761-7. doi: 10.1016/j.jplph.2004.01.010.
Seeds of common buckwheat (Fagopyrum esculentum) contain valuable nutritive substances but also allergenic proteins that cause hypersensitive reactions. Thus, the development of hypoallergenic buckwheat would make this important pseudo-cereal available to allergic people. A major allergenic protein of buckwheat is Fag e 1. We isolated the respective cDNA, coding for a 22 kDa protein, from a recently developed autogamous strain of common buckwheat and confirmed its immunoglobulin E (IgE)-binding activity using recombinant Fag e 1 and sera of allergic patients. The derived amino acid sequence from Fag e 1 cDNA was used to synthesize an overlapping peptide library on nitrocellulose membranes for the determination of the Fag e 1 epitopes. We identified eight epitopes and the critical amino acids for IgE-binding within the epitopes. This epitope analysis of a major allergenic protein of buckwheat should help therapeutic efforts and aid in the development of hypoallergenic buckwheat.
普通荞麦（苦荞麦）种子含有宝贵的营养物质，但也含有会引发过敏反应的致敏蛋白。因此，开发低致敏性荞麦将使这种重要的假谷物可供过敏人群食用。荞麦的一种主要致敏蛋白是Fag e 1。我们从最近培育出的普通荞麦自交系中分离出了编码一种22 kDa蛋白的相应cDNA，并使用重组Fag e 1和过敏患者血清证实了其免疫球蛋白E（IgE）结合活性。利用Fag e 1 cDNA推导的氨基酸序列在硝酸纤维素膜上合成了一个重叠肽库，用于确定Fag e 1表位。我们鉴定出了8个表位以及这些表位内与IgE结合相关的关键氨基酸。对荞麦主要致敏蛋白的这种表位分析应有助于治疗研究，并有助于低致敏性荞麦的开发。
