Identification of a human epitope in hepatitis C virus (HCV) core protein using a molecularly cloned antibody repertoire from a non-symptomatic, anti-HCV-positive patient.

Two recombinant Fabs specific for aa 2-20 of the HCV core protein were both inhibited from binding to HCV core aa 1-48. However, it was deduced that the two different Fabs (FabC14 and rFabC3) recognized two different motifs in the region spanned by C2-20 peptide as FabC14 did not recognize C2-20 bound to the solid phase. Thus, the conformation of the motif recognized by rFabC14 may have ben modified when the peptide was bound to solid phase.