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.

针对丙型肝炎病毒（HCV）包膜的单克隆抗体（mAb）主要针对包膜蛋白2（E2）产生，而包膜蛋白1（E1）的抗原表位尚未完全鉴定。在这里，我们描述了从HCV基因型1b感染患者中产生的人类mAb（称为A6）的详细特征。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。表位作图鉴定了跨越E1 N末端区域内第230-239位氨基酸的区域，这对结合至关重要。与该表位结合的抗体不是构象依赖性的。中和试验表明，mAb A6缺乏中和能力，并且不会干扰已知中和抗体的活性。总之，