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

• Published in: Biological chemistry Vol. 379; no. 1; pp. 65 - 70
• Main Authors: Demangel, C, Rouyre, S, Alzari, P M, Nato, F, Longacre, S, Lafaye, P, Mazie, J C
• Format: Journal Article
• Language: English
• Published: Germany De Gruyter 01.01.1998
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Antibodies, Monoclonal - chemistry; Antibodies, Monoclonal - immunology; Antigens, Protozoan; Antigens, Protozoan - immunology; Bacteriophages; Bacteriophages - genetics; Biochemistry, Molecular Biology; Bioinformatics; Biological Physics; Cellular Biology; Chemical Sciences; Computer Science; Cristallography; Immunoglobulin Variable Region; Immunoglobulin Variable Region - immunology; Life Sciences; Malaria Vaccines; Malaria Vaccines - immunology; Merozoite Surface Protein 1; Mice; Mice, Inbred Strains; Models, Molecular; Molecular Sequence Data; Peptide Fragments; Peptide Fragments - chemistry; Peptide Fragments - immunology; Peptide Library; Physics; Plasmodium cynomolgi; Plasmodium cynomolgi - chemistry; Plasmodium cynomolgi - immunology; Plasmodium vivax; Plasmodium vivax - immunology; Protein Precursors; Protein Precursors - immunology; Protozoan Proteins; Protozoan Proteins - immunology; Sequence Alignment; Sequence Analysis, DNA; Structural Biology; Monoclonal antibodies; Phage display; Vaccine; Malaria; Mimotopes

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 the 42 kDa C-terminal fragment of the major merozoite surface protein 1 of Plasmodium vivax (Pv42). In order to investigate the use of such...