Maltodextrin-binding protein hybrids carrying epitopes from the preS2 region of hepatitis B virus: expression, antibody-binding and preliminary crystallographic studies

• Published in: Protein engineering Vol. 10; no. 2; pp. 175 - 180
• Main Authors: Vulliez-le Normand, B, Saul, F A, Martineau, P, Lema, F, Hofnung, M, Bentley, G A
• Format: Journal Article
• Language: English
• Published: England 01.02.1997
• Subjects: Amino Acid Sequence; Antibodies, Monoclonal; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - immunology; Binding Sites; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - immunology; Cross Reactions; Crystallography, X-Ray; Epitopes - chemistry; Epitopes - genetics; Epitopes - metabolism; Escherichia coli Proteins; Hepatitis B Antibodies - metabolism; Hepatitis B Surface Antigens - chemistry; Hepatitis B Surface Antigens - genetics; Hepatitis B Surface Antigens - metabolism; Models, Molecular; Molecular Sequence Data; Molecular Structure; Periplasmic Binding Proteins; Protein Conformation; Protein Engineering; Protein Precursors - chemistry; Protein Precursors - genetics; Protein Precursors - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - immunology
• ISSN: 0269-2139; 1741-0126; 1741-0134
• DOI: 10.1093/protein/10.2.175

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.