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本文报道用分子生物学技术构建了含有乙型肝炎病毒（HBV）数个表面抗原蛋白表位的重组多肽（MEP-1）,并研究了它的免疫学特性。 MEP-1由100个氨基酸构成,其中,1～36位氨基酸来源于HBsAg前SI的12～47位氨基酸,包括T辅助（Th）细胞表位、中和表位和使HBV吸附于肝细胞的序列;39～64位氨基酸来自HBsAg前S2 120～145位氨基酸,包括Th细胞表位、中和表位和结合聚合人血清白蛋白的位点;65～74和77～100位氨基酸分别来自S蛋白的19～28位氨基酸（代表Th细胞表位）和124～147位氨基酸（0S）,后者可自行装配成天然HBV的构象依赖性、组特异性表位。MEP-1中不同序列之间均插入2个甘氨酸残基,作为不同表位的间隔物。 将MEP-1免疫小鼠和家兔,经ELISA检测,两种动物均产生了高滴度抗MEP-1抗体,Balb/c和C57B1/6小鼠免疫后抗体滴度>1/10万。对不同表位的特异性抗体水平的分析显示,高水平抗体主要由前S1序列诱导,抗OS（124～147）肽的抗体水平次之,而抗前S2抗体水平很低或呈阴性。分别以前S1/前 S2、前S2/S（19～28）和S（19～28）/OS（124～147）连接点的合成肽（包括两侧至
This paper reports the construction of a recombinant polypeptide (MEP-1) containing several surface antigen epitopes of hepatitis B virus (HBV) using molecular biology techniques and its immunological properties. MEP-1 consists of 100 amino acids, of which amino acids 1-36 are derived from amino acids 12-47 of the pre-HBsAg, including T helper (Th) cell epitopes, neutralizing epitopes, and adsorption of HBV to hepatocytes Sequence; amino acids 39-64 are from amino acids 120- 145 of pre-S2 of HBsAg, including Th cell epitopes, neutralizing epitopes and sites of binding to polymeric human serum albumin; amino acids 65-74 and 77-100 are derived from S Protein amino acids 19-28 (representing the Th cell epitope) and amino acids 124-147 (OS), which self-assemble into the conformational, group-specific epitopes of native HBV. Two glycine residues were inserted between different sequences in MEP-1 as spacers for different epitopes. MEP-1 immunized mice and rabbits were tested by ELISA. Both animals had high titers of anti-MEP-1 antibody. Balb / c and C57B1 / 6 mice had antibody titers> 1/10 million after immunization. Analysis of specific antibody levels for different epitopes showed that high levels of antibodies were predominantly induced by the preS1 sequence, followed by antibodies against OS (124-147), whereas anti-preS2 antibodies were low or negative. Synthetic peptides (including both sides to the junction of S1 / S2, S2 / S (19-28) and S (19-28) / OS