Identification of<i>Plasmodium</i>GAPDH epitopes for generation of antibodies that inhibit malaria infection

Abstract

<i>Plasmodium</i> 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 <i>Plasmodium</i> 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 <i>Plasmodium</i> GAPDH interacts with the Kupffer CD68 receptor, and identify two epitopes within this region as candidate antigens for the development of antibodies that inhibit <i>Plasmodium</i> infection.