Abstract
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.
- Received June 19, 2018.
- Revision received September 5, 2018.
- Accepted September 7, 2018.
- © 2018 Cha et al.
This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/).