Antibodies to malaria peptide mimics inhibit Plasmodium falciparum invasion of erythrocytes.

This peptide is derived from a random 20-mer peptide library. It mimics a conformational epitope on P.falciparum AMA-1 protein, recognized by the inhibitory rat mAb 4G2dc1. The library was constructed with random 20-mer peptides fused to the N-terminus of protein III of phage M13. Isolated after 6 rounds of panning with mAb 4G2dc1 (directed towards an undefined conformational epitope on Plasmodium falciparum AMA-1, with inhibitory activity on merozoite invasion into erythrocytes), the phage particle carrying this peptide is specifically recognized in ELISA by AMA-1 specific Abs affinity purified from malaria exposed-donors sera. Also free-peptide specific reactivity is seen in total serum (15/24 responders), with titers lower but correlating with those towards AMA-1 protein.