Abstract
Five hybrid constructions of maltodextrin-binding protein (MBP), each containing an inserted epitope(s) from the preS2 region of the envelope proteins of hepatitis B virus (HBV), have been expressed. The anti-preS2 monoclonal antibody S2.3 was shown to cross-react with the MBP hybrid constructions, demonstrating that the epitopes presented by these recombinant proteins mimic the antigenic behaviour of the native viral antigen. In addition, all five hybrid proteins have been crystallized. Preliminary structural solutions obtained by molecular replacement indicate that the native conformation of MBP is preserved in the hybrid constructions despite the significant length of the epitope insertions.
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