【摘要】：為鑒定鴨坦布蘇病毒(duck Tembusu virus,DTMUV)的B細(xì)胞抗原表位,以純化的DTMUV YY5株為抗原制備了2株單克隆抗體AE4和BD10,研究證實(shí)BD10為線性化表位,其結(jié)合的抗原表位位于E蛋白的第三結(jié)構(gòu)域(DomainⅢ,D_Ⅲ)。將DTMUV E蛋白D_Ⅲ結(jié)構(gòu)域基因截短為具有末端相互重疊的15段,與MBP融合表達(dá)后以單克隆抗體BD10進(jìn)行肽庫掃描,結(jié)果篩選出DTMUV一個B細(xì)胞線性表位_(385)LVGSGKGQI_(393)(EP385)。該表位原核融合表達(dá)產(chǎn)物免疫小鼠制備的抗體,能夠和DTMUV E蛋白反應(yīng),表明EP385表位具有良好的免疫原性,可為DTMUV多肽疫苗的研制及特異血清學(xué)診斷方法的開發(fā)奠定基礎(chǔ)。
[Abstract]:In order to identify B cell epitopes of duck tambusuvirus (duck Tembusu virus,DTMUV), two monoclonal antibodies, AE4 and BD10, were prepared with purified DTMUV YY5 strain as antigen. The results showed that BD10 was a linearized epitope. The binding epitopes are located in the third domain of E protein (Domain 鈪，

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