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Diversity of core antigen epitopes of hepatitis B virus

机译：乙型肝炎病毒核心抗原表位的多样性

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Core antigen (cAg), the viral capsid, is one of the three major clinical antigens of hepatitis B virus. cAg has been described as presenting either one or two conformational epitopes involving the "immunodominant loop." We have investigated cAg antigenicity by cryo-electron microscopy at approximate to11-Angstrom resolution of capsids labeled with monoclonal Fabs, combined with molecular modeling, and describe here two conformational epitopes. Both Fabs bind to the dimeric external spikes, and each epitope has contributions from the loops on both subunits, explaining their discontinuous nature: however, their binding aspects and epitopes differ markedly. To date, four cAg epitopes have been characterized: all are distinct. Although only two regions of the capsid surface are accessible to antibodies, local clustering of the limited number of exposed peptide loops generates a potentially extensive set of discontinuous epitopes. This diversity has not been evident from competition experiments because of steric interference effects. These observations suggest an explanation for the distinction between cAg and e-antigen (an unassembled form of capsid protein) and an approach to immunodiagnosis, exploiting the diversity of cAg epitopes. [References: 42]
机译：核心抗原（cAg），病毒衣壳，是乙型肝炎病毒的三种主要临床抗原之一。 cAg被描述为呈递一个或两个构象表位，涉及“免疫优势环”。我们已经通过冷冻电子显微镜在大约11埃的衣壳单克隆抗体标记衣壳分辨率上研究了cAg的抗原性，并结合了分子模型，并在此描述了两个构象表位。两种Fab均与二聚体外部尖峰结合，并且每个表位均来自两个亚基上的环，这说明了它们的不连续性：但是，它们的结合方式和表位明显不同。迄今为止，已表征了四个cAg表位：所有特征都不同。尽管衣壳表面只有两个区域可被抗体接近，但有限数量的暴露肽环的局部聚类产生了潜在的广泛的不连续表位集。由于空间干扰效应，这种多样性在竞争实验中并不明显。这些观察结果为解释cAg和e-抗原（一种未组装的衣壳蛋白）之间的区别提供了一种解释，并为利用cAg表位的多样性进行免疫诊断提供了一种方法。 [参考：42]

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