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Position: Home > Articles > Identification of the Critical Amino Acids of IgE-Binding Epitopes in α-Lactalbumin FOOD SCIENCE 2017,38 (11) 1-5

牛乳α-乳白蛋白IgE线性表位的关键氨基酸识别

作  者:
丛艳君;陈澍;李晔;于晓凤;李林峰
单  位:
北京工商大学食品学院食品添加剂与配料北京高校工程研究中心;北京友谊医院皮肤科
关键词:
牛乳过敏;α-乳白蛋白;作用表位;关键氨基酸
摘  要:
α-乳白蛋白是引起牛乳过敏的主要过敏原之一。识别α-乳白蛋白作用表位及影响致敏性的关键氨基酸,对于揭示α-乳白蛋白致敏机理及低致敏乳制品的开发具有重要的意义。本研究采用固相合成技术合成α-乳白蛋白系列多肽,以牛乳过敏患者血清为探针,通过酶联免疫吸附分析法识别α-乳白蛋白的作用表位和关键氨基酸。结果表明:免疫球蛋白(immunoglobulins,Ig)E作用表位的氨基酸序列定位为aa1-15、aa6-20、aa46-60、aa71-85和aa101-115。α-乳白蛋白IgE作用表位关键氨基酸为第8位的缬氨酸、第9位的苯丙氨酸、第10位的精氨酸、第103位的酪氨酸、第105位的亮氨酸和第107位组氨酸。本研究可以为过敏原c DNA克隆以激活T细胞、降低IgE结合能力提供重要思路。
译  名:
Identification of the Critical Amino Acids of IgE-Binding Epitopes in α-Lactalbumin
作  者:
CONG Yanjun;CHEN Shu;LI Ye;YU Xiaofeng;LI Linfeng;Beijing Higher Institution Engineering Research Center of Food Additives and Ingredients, College of Food Science,Beijing Technology and Business University;Department of Dermatology,Beijing Friendship Hospital;
关键词:
cow milk allergy;;α-lactalbumin;;epitope;;critical amino acid
摘  要:
α-Lactalbumin represents one of the major allergens causing cow milk allergy. The identification of the epitopes of α-lactalbumin and the critical amino acids for its allergenicity is of great significance for understanding the mechanism of action of α-lactalbumin and developing hypoallergenic dairy products. In this study, a series of peptides were synthesized by a solid phase method for the characterization of immunological epitopes and critical amino acids. The immunoglobulin(Ig) E-binding epitopes were immunolabeled with individual sera from cow milk-allergic patients as probes by enzyme linked immunosorbent assay(ELISA). Alanine scanning of immunodominant epitopes was used to identify the critical amino acids(aa). The results showed that IgE-binding epitopes were located within the sequences of aa1-15, aa6-20, aa46-60, aa71-85 and aa101-115. Our initial data revealed that Val~8, Phe~9, Arg~(10), Tyr~(103), Leu~(105) and His~(107) were the critical amino acids for IgE-binding epitopes. This study will provide the necessary information to alter the c DNA to encode a protein capable of activating milk-specific T cells, but with reduced IgE-binding capacity.

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