Plasmodium falciparum is the most virulent human malaria parasite, accounting for the overwhelming majority of malaria-related deaths each year. P. falciparum parasites invade red blood cells (RBCs) and extensively modify the structure and morphology of their host cell to better accommodate the growing parasite during its approximate 48 hour intra-erythrocytic cycle. Fundamental to these remodelling processes is the export of a diverse group of parasite proteins to various locations within the host cell cytoplasm. The proper export of these proteins is a challenge - even prior to the complexities of sorting of proteins within the host RBC cytoplasm, export of these parasite proteins is first complicated by the fact that the parasite resides within a parasitophorous vacuole (PV). Proteins need to be exported out of the parasite endomembrane system, to cross the parasite plasma membrane (PPM) so as to enter the PV lumen, and finally to passage across the PV membrane (PVM) into the host cytoplasm. Protein unfolding and refolding has been demonstrated to be vital for successful export across these compartments 1 2 - an observation supported by the fact that over one third of proteins in the PV lumen are molecular chaperones 3 . In this work we have examined a previously poorly characterised parasite-encoded molecular chaperone, called Pfj4, and examined its potential role in the export of the major virulence protein, PfEMP1, between the parasite and host cell cytoplasm. Pfj4 is trafficked to compartments at the parasite periphery soon after invasion, and may play a role in early export of parasite proteins. Targeting the export of parasite proteins would ablate parasite virulence.