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Significance Epitope III, a segment on the E2 glycoprotein of the hepatitis C virus (HCV) which binds to the host receptor CD81, is a key target for antibodies to block HCV entry. By solving the atomic structure of epitope III bound to a site-specific neutralizing antibody, mAb1H8, we showed that the epitope can adopt two distinct conformations by moving the side chains of its amino acids, allowing it to bind with either mAb1H8 or CD81. The coexistence of different conformational states of epitope III suggests its possible role in the regulation of antibody responses. These findings should help to design strategies to control HCV infection by tipping the balance toward epitope III conformations that favor antibody recognition rather than CD81 binding.

A conserved epitope III on hepatitis C virus E2 protein has alternate conformations facilitating cell binding or virus neutralization