The analysis of the epitope structures of food allergens by using the synthetic peptides.

阐明过敏原表位结构对预防和治疗食物过敏具有重要意义。在这项研究中，我们检查了酪蛋白的结构，牛乳中的强效过敏原之一。利用人工合成的重叠肽和酶切片段确定了牛s1-酪蛋白（s1-CN）被T细胞和B细胞识别的完整位点。结果表明：1)51 - cn上的有限位点能被T细胞和B细胞识别；2)在具有独立单倍型的3个小鼠品系中，s1-CN上这些识别位点的谱图相似。在分子水平上分析了-酪蛋白（-cn）单克隆抗体（MAb1C3）与其片段的相互作用。结果表明，氨基酸残基194Gln、200Pro和202Arg对与MAb1C3结合的贡献较大，而193Tyr和201Val的贡献不如前者。这些食物过敏原表位结构的信息可能有助于理解免疫应答中的抗原识别以及食物过敏中的超敏反应。

It is important for prevention and cure of food allergy to elucidate the epitope structures of the allergens. In this study, we examined the structures of casein, one of potent allergens in bovine milk.The full profiles of the sites on bovin s1-casein ( s1-CN) recognized by T and B cells were determined by using synthetic overlapping peptides and enzymatically digested fragments. It was shown that 1) limited sites on s1-CN are recognized by T and B cells; 2) the profiles of these recognition sites on s1-CN are similar in three mouse strains that have independent haplotypes.The interaction between monoclonal antibody (MAb1C3) to -casein ( -cn) and its fragments was analyzed at the molecular level. As a result, it was shown that the amino acid residues, 194Gln, 200Pro and 202Arg, contributed largely to the binding to MAb1C3 and the contributions of 193Tyr and 201Val were inferior to the formers.This information on the epitope structure of food allergens may be useful in understandind the antigen recognition in the immune response as well as the hypersensitivity in food allergy .