Phage-displayed mimotopes elicit monoclonal antibodies specific for a malaria vaccine candidate.

摘要: The phage-displayed peptide CGRVCLRC (C15) has been isolated from a random library by affinity screening with the D14-3 monoclonal antibody, which was raised to 42 kDa C-terminal fragment of major merozoite surface protein 1 Plasmodium vivax (Pv42). In order investigate use such mimotopes as possible vaccine components, we studied antibody response in Biozzi mice immunized C15. High titers antibodies cross-reacting Pv42 were generated and IC50 all immune sera 5 x 10(-9) M range. Two that specifically bind isolated. Although these mAbs had lower for when compared D14-3, they reproduced cross-reactivity equivalent P. cynomolgi, close relative vivax. DNA sequence analysis showed similarities between germline genes canonical CDR conformations three antibodies, but molecular modeling failed reveal common structural features their paratopes could account patterns. These data demonstrate selected repertoires do not necessarily represent equivalents original antigen provide functional images replace it development.