【摘要】 猪瘟病毒(CSFV)囊膜结构糖蛋白E2(gp55)是激发保护性免疫应答的主要抗原蛋白。Erns和E2与细胞表面受体的相互作用介导病毒对细胞的感染过程。采用抗CSFV中和性单克隆抗体c24/10,淘选噬菌体展示的12肽随机肽库,结合噬菌体拟位免疫反应性分析结果,对CSFVE2蛋白中和表位进行定位。结果表明:E2蛋白的SPT-TLR基序(832～837位氨基酸)构成CSFV特异性线性中和表位,基序的第一、二、三位氨基酸是表位与单克隆抗体c24/10结合所必需的氨基酸,也是表位的关键性氨基酸。更多还原

【Abstract】 The structural envelope glycoprotein E2(gp55)of CSFV is the major protein responsible for eliciting and conferring protective immunity. Infection of cells by CSFV is mediated by the interaction of E2 and Erns with cell surface receptor.In this paper, we report the mapping of neutralizing epitope of E2 by screening a 12-mer random peptide phage display library using the neutralizing MAb c24/10 raised against CSFV glycoprotein E2, and analysis of immunoreactivities between MAb c24/10 and phage mimotopes. The results showed SPTTLR motif located at aa832 - aa837 of E2 protein constituted a CSFV specific linear neutralizing epitope. Amino acids of first site to third site among the motifs are essential for binding between the epitope and MAb c24/10,and also are critical residues of the epitope.更多还原