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出 处:《生物化学与生物物理进展》2005年第6期523-528,共6页Progress In Biochemistry and Biophysics
基 金:国家自然科学基金资助项目(30070719)~~
摘 要:TLR-2(Toll-likereceptor2)是介导天然免疫的重要模式识别分子,可参与识别多种病原体及其产物.为探索被TLR-2所识别配基的结构共性,以真核细胞表达的人TLR-2胞外段蛋白(A26 ̄T588)为钓饵筛选噬菌体12肽库,获得一高度保守的阳性噬菌体克隆P12-1,实验发现P12-1可与不同形式的TLR-2胞外段结合,并且可刺激细胞分泌TNFα,提示P12-1可能模拟TLR-2配基的结构与生物学活性.Toll-like receptor 2 is an important pattern recognition molecule of innate immune, which could recognize diverse pathogens and their products. Using the eukaryotic expression TLR-2 extracellular fragment as target to screen peptide mimics to ligand of TLR-2 from Ph.D.-12 phage display peptide library, 20 of positive phage clones were sequenced, which shared a very conservative sequence and was named as P12-1. Biotinylated peptide P12-1 could bind with different form of TLR-2 extracellular fragment, and also stimulate THP-1/CD14 cells to secrete TNF alpha. These results indicated that P 12-1 could mimic the structure and activity of ligand of TLR-2.
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