Plasmodium falciparum is a protozoan parasite involved in the most serious form of cerebral Malaria. During the infection, the parasite invades red blood cells and alters their surface properties. This modification causes cytoadherence of the host cells to endothelial cells of the brain venules, which induces microvascular obstruction and severe clinical manifestations. The parasite is able to assemble a multiprotein adhesion complex at the host red blood cell membrane, which has for principal component the P. falciparum erythrocyte membrane protein-1 (PfEMP1). During the intra-erythrocytic cycle, the parasite develops within a parasitophorous vacuole (PV). PfEmp1 must be exported beyond that vacuole to induce modifications in the RBC, however little is known about the mechanism for this export. Previous studies have revealed that PfEMP1 exhibits a necklace of beads pattern at the surface of the parasitophorous vacuole. Interestingly, the protein PfGCN20 was found concentrated in similar bulging regions of the PV and appears related to the ATP-hydrolysing subunit of some bacterial ABC transporters. This suggests that PfGCN20 could be involved in the ATP-binding and hydrolysing subunit of a multimeric ABC transport system and may have a role in the PfEmp1 translocation across the PV membrane. The aim of the project is to shed some light on the role of PfGCN20 in the trafficking of PfEmp1 and its interaction with other proteins involved in the putative ABC transport system. The first set of experiments is focused on design, testing and optimisation of an antibody specific against PfGCN20, to obtain an efficient tool for detection of the protein in P. falciparum. The antibody will then be used to characterize the subcellular localization of GCN20 at different stages of the parasite lifecycle and its interaction with PfEMP1. To complete the visualisation of the protein, PfGCN20 fusion minigene transfectant tagged with GFP will also be generated.