Ulrich R, Borisova G P, Gren E, Berzin I, Pumpen P, Eckert R, Ose V, Siakkou H, Gren E J, von Baehr R
Institute of Virology, Charité, Berlin, Federal Republic of Germany.
Arch Virol. 1992;126(1-4):321-8. doi: 10.1007/BF01309705.
A Gag protein segment of human immunodeficiency virus 1 (HIV-1) has been fused to a C terminally truncated core antigen of hepatitis B virus (HBcAg) using an E. coli expression system. Fusion of 90 amino acids of HIV-1 Gag protein to HBcAg still allowed the formation of capsids presenting on their surface epitopes of HIV-1 core protein, whereas fusion of 317, 189, or 100 amino acids of Gag prevented self-assembly of chimeric particles. Mice immunized with recombinant particles emulsified with Freund's complete adjuvant (CFA) or aluminium hydroxide developed high anti-HBcAg titers. However, anti-HIVp24 antibodies were detected only in mice inoculated with immunogen emulsified with CFA.
利用大肠杆菌表达系统,将人类免疫缺陷病毒1型(HIV-1)的一段Gag蛋白与乙型肝炎病毒(HBcAg)C端截短的核心抗原融合。将HIV-1 Gag蛋白的90个氨基酸与HBcAg融合,仍能形成在其表面呈现HIV-1核心蛋白表位的衣壳,而融合317、189或100个Gag氨基酸则会阻止嵌合颗粒的自组装。用弗氏完全佐剂(CFA)或氢氧化铝乳化的重组颗粒免疫的小鼠产生了高抗-HBcAg滴度。然而,仅在接种了用CFA乳化的免疫原的小鼠中检测到抗-HIV p24抗体。