Lee M K, Kim K L, Hahm K S, Yang K H
Genetic Engineering Research Institute, KIST, Yusong, Taejon, Korea.
Biochem Mol Biol Int. 1994 Aug;34(1):159-68.
Peptide antigenicity against the pre-S2 region of the hepatitis B virus surface antigen was studied using a pre-S2 specific anti-hepatitis B virus mouse monoclonal antibody (H8 mAb) and synthetic peptides by competitive ELISA. The mAb showed preferences for long peptides with the sequence 120/123-145, though the mAb binding region was located in the sequence 130-145 from the analysis of a conjugation study. The N-terminal residues 120/123-129 play an important role for the maintenance of the highly antigenic structure of the B cell epitope. Among these, the N-terminal hydrophilic residues 124-126 and hydrophobic residue 127 were important, whereas residues 120-122 did not affect antigenicity. Residues 131 and 141 appeared to be critical for the mAb binding. The relationship between peptide structure and antigenicity was also investigated by probing the secondary structure of the peptides by circular dichroism. Highly antigenic peptides elicited more ordered structure in 20% trifluoroethanol than less antigenic peptides. The results suggested that peptide antigenicities against H8 mAb are closely related to the B-cell epitope conformations of peptides.
利用一种前S2特异性抗乙肝病毒小鼠单克隆抗体（H8单克隆抗体）和合成肽，通过竞争性酶联免疫吸附测定法研究了针对乙肝病毒表面抗原前S2区域的肽抗原性。该单克隆抗体对序列为120/123 - 145的长肽表现出偏好，不过从结合研究分析来看，单克隆抗体的结合区域位于序列130 - 145。N端残基120/123 - 129对维持B细胞表位的高抗原性结构起重要作用。其中，N端亲水性残基124 - 126和疏水性残基127很重要，而残基120 - 122不影响抗原性。残基131和141似乎对单克隆抗体的结合至关重要。还通过圆二色性探测肽的二级结构来研究肽结构与抗原性之间的关系。与抗原性较低的肽相比，高抗原性肽在20%三氟乙醇中引发的结构更有序。结果表明，针对H8单克隆抗体的肽抗原性与肽的B细胞表位构象密切相关。
