将鳗鲡疱疹病毒(AngHV)福建株(AngHV-FJ)ORF51基因克隆至原核表达载体pGEX-4T-2中,构建表达质粒pGEX-4T-2-ORF51,将其转化至表达菌株E.coli BL21 (DE3)中,IPTG诱导后,收集表达菌体,进行SDS-PAGE分析和免疫印迹试验验证,结果表明,获得了高效表达的AngHV-FJ ORF51融合蛋白.经割胶回收纯化,获得高纯度的融合表达蛋白.用纯化的表达蛋白免疫新西兰大白兔,获得了高效价的兔抗ORF51多克隆抗体.这为进一步研究ORF51蛋白的结构和功能及开展AngHV病的防治研究提供了重要的研究基础.
AngHV-FJ ORFS1 gene was inserted in prokaryofie expression vector pGEX-4T-2 to construct expression plasmid pGEX- 4T-2-ORFS1, and then the plasmid was transformed into E. coli BI21 (DE3), and induced by IPTG. SDS-PAGE and Western blot analysis confirmed that AngHV-FJ ORFS1 protein was highly expressed in E. coli BI21 (DE3). The expressed ORFS1 protein was obtained by gel extraction purification, and used to immunize rabbit, and high titer rabbit anti-ORFS1 polyelonal antibody was ob- tained. The results provided fundamental data and materials for the farther study on the structure and function of ORFS1 protein and AngHV prevention.