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. Antibodies were affinity-purified with AMA-1 protein from peptide-immunized rabbits sera. They are able to specifically recognize bacterially expressed recombinant AMA-1 corresponding to 4 different P.falciparum isolates (3D7, D10, HB3 and W2mef), by ELISA, and AMA1 (3D7), but not reduced and alkylated AMA1, by immunoblot. This reactivity is identical to that of rat mAb 4G2dc1, used to isolate this peptide from a random peptide library.