Department of Clinical Chemistry, Microbiology and Immunology, Ghent University, Ghent, Belgium; Therapeutic Chemistry Department, National Research Centre (NRC), Dokki, Cairo, Egypt.
Department of Clinical Chemistry, Microbiology and Immunology, Ghent University, Ghent, Belgium.
Virology. 2018 Jan 15;514:30-41. doi: 10.1016/j.virol.2017.10.019. Epub 2017 Nov 10.
Monoclonal antibodies (mAbs) targeting the hepatitis C virus (HCV) envelope have been raised mainly against envelope protein 2 (E2), while the antigenic epitopes of envelope protein 1 (E1) are not fully identified. Here we describe the detailed characterization of a human mAb, designated A6, generated from an HCV genotype 1b infected patient. ELISA results showed reactivity of mAb A6 to full-length HCV E1E2 of genotypes 1a, 1b and 2a. Epitope mapping identified a region spanning amino acids 230-239 within the N-terminal region of E1 as critical for binding. Antibody binding to this epitope was not conformation dependent. Neutralization assays showed that mAb A6 lacks neutralizing capacity and does not interfere with the activity of known neutralizing antibodies. In summary, mAb A6 is an important tool to study the structure and function of E1 within the viral envelope, a crucial step in the development of an effective prophylactic HCV vaccine.
单克隆抗体（mAbs）针对丙型肝炎病毒（HCV）包膜已主要针对包膜蛋白 2（E2），而包膜蛋白 1（E1）的抗原表位尚未完全确定。在这里，我们描述了一种人源 mAb 的详细特征，该 mAb 由感染 HCV 基因型 1b 的患者产生，命名为 A6。ELISA 结果显示 mAb A6 对基因型 1a、1b 和 2a 的全长 HCV E1E2 具有反应性。表位作图确定 E1 的 N 端区域内氨基酸 230-239 内的一个区域对于结合至关重要。抗体与该表位的结合不依赖于构象。中和测定表明 mAb A6 缺乏中和能力，并且不干扰已知中和抗体的活性。总之，mAb A6 是研究病毒包膜中 E1 的结构和功能的重要工具，这是开发有效预防性 HCV 疫苗的关键步骤。
