Mapping B-cell epitopes of hepatitis C virus E2 glycoprotein using human monoclonal antibodies from phage display libraries

Clinical and experimental evidence indicates that the hepatitis C virus (HC V) E2 glycoprotein (HCV/E2) is the most promising candidate for the develop ment of an effective anti-HCV vaccine. Identification of the human epitopes that are conserved among isolates and are able to elicit protective antibo dies would constitute a significant step forward. This work describes the m apping of the B-cell epitopes present on the surface of HCV/E2, as recogniz ed by the immune system during infection, by the analysis of the reciprocal interactions of a panel of human recombinant Fabs derived from an HCV-infe cted patient. Three unrelated epitopes recognized by antibodies with no neu tralization-of-binding (NOB) activity were identified; a fourth, major epit ope was defined as a clustering of minor epitopes recognized by Fabs endowe d with strong NOB activity.