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Mapping B-Cell Epitopes of Hepatitis C Virus E2 Glycoprotein Using Human Monoclonal Antibodies from Phage Display Libraries

机译:使用来自噬菌体展示库的人类单克隆抗体定位丙型肝炎病毒E2糖蛋白的B细胞表位

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摘要

Clinical and experimental evidence indicates that the hepatitis C virus (HCV) E2 glycoprotein (HCV/E2) is the most promising candidate for the development of an effective anti-HCV vaccine. Identification of the human epitopes that are conserved among isolates and are able to elicit protective antibodies would constitute a significant step forward. This work describes the mapping of the B-cell epitopes present on the surface of HCV/E2, as recognized by the immune system during infection, by the analysis of the reciprocal interactions of a panel of human recombinant Fabs derived from an HCV-infected patient. Three unrelated epitopes recognized by antibodies with no neutralization-of-binding (NOB) activity were identified; a fourth, major epitope was defined as a clustering of minor epitopes recognized by Fabs endowed with strong NOB activity.
机译:临床和实验证据表明,丙型肝炎病毒(HCV)E2糖蛋白(HCV / E2)是开发有效抗HCV疫苗的最有希望的候选人。鉴定分离株中保守的并且能够引发保护性抗体的人表位将是向前迈出的重要一步。这项工作通过分析一组源自HCV感染患者的人类重组Fab的相互作用,描述了在感染过程中被免疫系统识别的HCV / E2表面B细胞表位的定位。鉴定出了被抗体识别的三个不相关的表位,这些抗体不具有中和结合(NOB)活性。第四,主要表位定义为由具有强NOB活性的Fab识别的次要表位的簇。

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