Abstract
Plasmodium falciparum (P. falciparum) completes the asexual phase of its life cycle inside human hepatocytes and red blood cells (RBCs). Following its entry into RBCs, P. falciparum transforms the infected cells through the extensive export of parasite-derived proteins. Exported proteins contain a conserved pentameric motif termed PEXEL ( P lasmodium Export Element). The mechanism of PEXEL-based export has been studied in detail using robust experimental methods. Interestingly, a few characterized exported proteins lack PEXEL motifs yet follow a similar route of trafficking. Several such PEXEL negative exported proteins (PNEPs) have been studied in P. falciparum. Here, we have summarized the current understanding of the mechanism of protein export and the structural diversity of discovered PNEPs and their functions in this parasite. Additionally, some remaining questions about the protein export mechanism in P. falciparum and in a few related apicomplexans have been discussed.