Neurath A R, Kent S B, Strick N
Science. 1984 Apr 27;224(4647):392-5. doi: 10.1126/science.6200931.
Immunodominant, disulfide-bond independent epitopes recognized by human antibodies to hepatitis B virus (HBV) are located within the 55-residue amino terminal portion (coded for by the pre-S region of HBV DNA) of minor HBV envelope components larger than the major protein constituents encoded by the S gene. A peptide having the sequence of the first 26 amino acids from the amino terminal methionine was synthesized and elicited antibodies (at dilutions of greater than or equal to 1 to 10(5) ) to the HBV envelope. These antibodies can be utilized for diagnostic tests. The immunogenicity of the peptide was substantially increased by covalent attachment to liposomes. The disulfide bond-independent determinants on sequences coded for by the pre-S gene may be more easily mimicked by peptide analogs than "conformational" determinants on the S-gene product.
被人类抗乙型肝炎病毒（HBV）抗体识别的免疫显性、不依赖二硫键的表位，位于比S基因编码的主要蛋白质成分稍大的HBV包膜次要成分的55个氨基酸的氨基末端部分（由HBV DNA的前S区域编码）内。合成了一种从氨基末端甲硫氨酸开始的前26个氨基酸序列的肽，并引发了针对HBV包膜的抗体（稀释度大于或等于1比10⁵）。这些抗体可用于诊断测试。通过与脂质体共价连接，该肽的免疫原性显著增强。前S基因编码序列上不依赖二硫键的决定簇可能比S基因产物上的“构象”决定簇更容易被肽类似物模拟。
