Dreesman G R, Sparrow J T, Frenchick P J, Kennedy R C
Adv Exp Med Biol. 1985;185:129-37. doi: 10.1007/978-1-4684-7974-4_8.
A synthetic hepatitis B surface antigen (HBsAg) peptide was prepared containing amino acid residues 122-137 of the major HBsAg polypeptide. This peptide was cyclized by the introduction of an intrachain disulfide bond between cysteine residues at positions 124 and 137 because previous studies had shown that intact disulfide bonds are critical for maintenance of HBsAg activity. An anti-HBs response was produced in mice by free peptide entrapped in liposomes. However, the immunogenicity was enhanced by aggregation into micelles, and by coupling to tetanus toxoid. Analysis of the peptide with a panel of monoclonal antibodies showed that peptide 122-137 contained a conformation (discontinuous) group a epitope and a sequential (continuous) subgroup y epitope. In addition, the cyclic peptide inhibited a human anti-HBs idiotype-anti-idiotype reaction with specificity for group a determinant(s). The potential for synthetic peptides for hepatitis B virus vaccine development is discussed.
制备了一种合成的乙型肝炎表面抗原（HBsAg）肽，其包含主要HBsAg多肽的122 - 137位氨基酸残基。由于先前的研究表明完整的二硫键对于维持HBsAg活性至关重要，因此通过在124位和137位的半胱氨酸残基之间引入链内二硫键使该肽环化。通过包裹在脂质体中的游离肽在小鼠体内产生了抗HBs反应。然而，通过聚集成胶束以及与破伤风类毒素偶联，免疫原性得到了增强。用一组单克隆抗体分析该肽表明，122 - 137肽包含一个构象（不连续）的a组表位和一个顺序（连续）的y亚组表位。此外，环肽抑制了对a组决定簇具有特异性的人抗HBs独特型 - 抗独特型反应。讨论了合成肽用于乙型肝炎病毒疫苗开发的潜力。
