甘露聚糖结合凝集素的丝氨酸蛋白酶结合位点初步研究  

Preliminary study on serine proteases binding sites on mannan-binding lectin

作　　者：蔡学敏[1] 赵娜[1] 左大明[1] 张丽芸[1] 陈政良[1] 

机构地区：[1]南方医科大学免疫学教研室,广州510515

出　　处：《现代免疫学》2009年第3期202-207,共6页Current Immunology

基　　金：国家自然科学基金资助项目(30371310);广东省自然科学基金研究团队项目(015003)

摘　　要：采用ELISA技术,建立人甘露聚糖结合凝集素(MBL)与MBL相关丝氨酸蛋白酶(MASP)结合的检测体系。设计合成一系列MBL胶原样区(CLR)的相应短肽进行抑制实验,发现MASP结合于MBL分子CLR中一个含16个氨基酸残基的区域,即成熟MBL肽链的第45～60位氨基酸残基,该区域位于Gly-X-Y三联体重复序列中Gly-Gln断裂的C端。还发现分别含1个突变残基的3种突变型(32Cys、34Asp和37Glu)MBL蛋白与MASP的结合具有类似野生型MBL蛋白的特征,但其结合能力明显降低,表明这3个突变残基位于MBL的MASP结合位点之外。Using the indirect enzyme-linked immunosorbent assay（ELISA）, a system detecting the interaction between human mannan-binding lectin （MBL） and MBL-associated serine proteases （MASPs） was established and a series of collagen like region （CLR） peptides were synthesized, which were assumed to block the MBL-MASP interaction in order to locate the MASPs binding sites on MBL. It was found that MASPs bind to a region of 16 amino acid residues, spanning amino acids 45 to 60 in mature polypeptide of human MBL, locating lies on the C-terminal side of the Gly-Gln interruption in the Gly-X-Y triplet repeat pattern of the collagen like domain. Three mutant MBL proteins, 32Cys, 34Asp and 37Glu MBL proteins, had the similar serine protease binding characteristic with wild type MBL but the binding was much weaker than that between wild type MBL protein and MASPs, demonstrating that these mutations locate outside the binding sites for MASPs.

关 键 词：甘露聚糖结合凝集素 丝氨酸蛋白酶 结合位点 合成肽 

分 类 号：R392.11[医药卫生—免疫学]