Identification of Plasmodium GAPDH epitopes for generation of antibodies that inhibit malaria infection

Plasmodium sporozoite liver infection is an essential step for parasite development in its mammalian host. Previously, we used a phage display library to identify mimotope peptides that bind to Kupffer cells and competitively inhibit sporozoite-Kupffer cell interaction. These peptides led to the identification of a Kupffer cell receptor-CD68-and a Plasmodium sporozoite ligand-GAPDH-that are required for sporozoite traversal of Kupffer cells and subsequent infection of hepatocytes. Here, we report that the C-terminal end of Plasmodium GAPDH interacts with the Kupffer CD68 receptor, and identify two epitopes within this region as candidate antigens for the development of antibodies that inhibit Plasmodium infection.