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研究了哺乳动物细胞(转基因GdSS1-18细胞系)分泌的乙型肝炎(乙肝)病毒表面S+PreS1融合抗原(SS1)纯品的理化及生物学性状,结果表明:经HPLC柱层析呈现一个对称峰,证明HBsAg颗粒所带电荷的均一性;SDS-PAGE出现P24及P27条带,未出现Gp30的条带,凝胶扫描分析其各条带分别各占22 3%、77 7%、0%;West ernblot试验证实,P27和Gp30能与S及S1抗体结合,而P24条带仅能与S抗体结合,表明S、PreS1是特异性条带;N-末端的氨基酸序列与所用目的基因编码的序列相同;乙肝SS1融合抗原在4℃储存较稳定。动物实验结果表明:与单纯含S基因的参比疫苗相比,含SS1融合基因疫苗免疫Balb/c小鼠既产生S抗体,又产生S1抗体,S抗体的ED50滴度与参比疫苗相似,S1抗体产生早于S抗体。
The physical and chemical properties of S + PreS1 fusion antigen (SS1) purified from mammalian cells (transgenic GdSS1-18 cell line) secreted by Hepatitis B virus (HBV) were studied. The results showed that one Symmetric peaks were used to demonstrate the charge uniformity of HBsAg particles. P24 and P27 bands appeared on SDS-PAGE and no Gp30 bands appeared. The bands of gel scanning analysis were 22 3% and 77 7% respectively %; West ernblot test confirmed that P27 and Gp30 with S and S1 antibody binding, and P24 band only with S antibody binding, indicating that S, PreS1 is a specific band; N-terminal amino acid sequence and the gene of interest coding The same sequence; hepatitis B SS1 fusion antigen stored at 4 ℃ more stable. Animal experiments showed that compared with the reference vaccine containing S gene alone, Balb / c mice immunized with the SS1 fusion gene vaccine both produced S antibody and S1 antibody. The ED50 titer of S antibody was similar to that of the reference vaccine, S1 antibodies develop earlier than S antibodies.