Converging antigenic structure of a recombinant viral peptide displayed on different frameworks of carrier proteins.

A peptide reproducing the G-H loop amino acid sequence of foot-and-mouth disease virus VP1 protein was fused to the solvent-exposed C-terminus of the bacteriophage P22 tailspike protein [Carbonell and Villaverde (1996) Gene, in press], a homotrimeric polypeptide with a strong beta-helical structure. This fusion does not interfere with the biological activities of the phage tail. The antigenic profile of the complex antigenic site A within the G-H loop has been determined by competitive ELISA with a panel of monoclonal antibodies directed against different overlapping B-cell epitopes. The antigenic data have been compared with those obtained with a set of 12 chimeric beta-galactosidases displaying the G-H loop on different exposed regions. A high coincidence has been evidenced between the antigenicity of the viral peptide fused to the phage protein and that of some peptides inserted in an exposed loop of the activating interface of beta-galactosidase. This indicates that completely different structural frameworks of carrier proteins can provide similar constraints that allow the recombinant peptide to successfully mimic the antigenicity, and probably conformational features, of the natural peptide on the virion surface.