人TLR-2胞外肽段的分段表达及其活性鉴定  

Prokaryotic expression and binding activity of different extracellular fragments of human TLR-2

作　　者：刘艳君[1] 罗冰[1] 赵文忠[2] 朱平[1] 富宁[1] 

机构地区：[1]南方医科大学免疫学教研室,广州510515 [2]中山大学医学院微生物学教研室,广州510080

出　　处：《现代免疫学》2006年第4期269-273,共5页Current Immunology

基　　金：国家自然科学基金资助项目(30400404);广东省自然科学基金资助项目(020017)

摘　　要：为深入研究TLR-2胞外肽段不同区域在配基识别过程中的功能,对TLR-2a(7M-225E)、TLR-2b(185L-392L)、TLR-2c(436E-595C)三个小片段进行克隆及原核表达,其中TLR-2a和TLR-2c得到成功克隆和表达,活性鉴定结果显示TLR-2a与商品抗TLR-2(179L-204I)多抗和抗His单抗反应良好,TLR-2c可以与抗His单抗反应,在配基结合实验中TLR-2a和TLR-2c都可与PGN和LTA结合,提示TLR-2对配基的识别为构像识别。In order to investigate the role of different extracellular fragments of TLR-2 in ligand recognition, three short fragments named as TLR-2a（7M-225E）, TLR-2b（1851.-392L）, and TLR-2c（436E-595C） were cloned and expressed in prokaryotic expression system. Recombinant proteins TLR-2a/His and TLR-2c/His were successfully purified from inclusion body. TLR-2a could bind with polyclonal antibody （TLR-2 against 179L-204I, Ab-1） and anti-His antibody, while TLR-2c could react with anti His antibody only. These results of ligand-binding assay indicate that both TLR-2a and TLR-2c can bind with PGN and LTA which are known as the important ligands from bacteria to TLR-2.

关 键 词：TLR-2肽段 原核表达 配基识别 

分 类 号：R392[医药卫生—免疫学]