Protein transport in the host cell cytoplasm and ATP-binding cassette proteins in Plasmodium falciparum-infected erythrocytes.

The main interest of our experiments is the study of ATP-binding cassette (ABC) proteins in Plasmodium parasites and their infected host cells. Here, we report on results obtained by studying the plasmodial PfGCN20 ABC protein. Employing immunomicroscopy and cell fractionation techniques, we found that PfGCN20 is localized to multiple regions of the infected erythrocyte, including membranous and non-membranous compartments inside and outside of the parasite cell. PfGCN20 was found to complement the function of its yeast homologue Gcn20p by acting as part of the yeast translation regulatory pathway. These results open up several hypotheses about a possible biological function of PfGCN20, such as being a component of plasmodial translation regulation, or functioning as an ATP-binding subunit of a multimeric ABC transporter, or acting as a molecular chaperone-like enzyme contributing to the protein translocation across multiple membranes in infected erythrocytes. More experiments are presently being performed to fully understand the biological function of this protein, abundant in multiple compartments of erythrocytes infected with the Plasmodium falciparum malaria parasite.