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

阐明食物过敏原的表位结构对食物过敏的防治具有重要意义。本研究利用人工合成的重叠肽和酶切片段，对牛乳中强过敏原酪蛋白（casein，CN）的结构进行了研究，确定了T细胞和B细胞识别牛s1-CN的全部位点。结果表明：（1）s1-CN上的有限位点能被T细胞和B细胞识别，（2）这些识别位点在3个具有独立单倍型的小鼠品系中的分布相似。结果表明，194 Gln、200 Pro和202 Arg对MAb 1C 3的结合贡献最大，193 Tyr和201 Val次之，这对了解食物过敏原的表位结构和免疫应答中的抗原识别以及食物过敏的超敏反应具有重要意义。

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 .