Background: Plasmodium, the causative agent of malaria, exports many proteins to the surface of the infected red blood cell (iRBC) in order to modify it toward a structure more suitable for parasite development and survival. One such exported protein, SURFIN_4.2, from the parasite of human malignant malaria, P. falciparum, was identified in the trypsin-cleaved protein fraction from the iRBC surface, and is thereby inferred to be exposed on the iRBC surface. SURFIN_4.2 also localize to Maurer’s clefts—parasite-derived membranous structures established in the RBC cytoplasm and tethered to the RBC membrane—and their role in trafficking suggests that they are a pathway for SURFIN_4.2 transport to the iRBC surface. It has not been determined the participation of protein domains and motifs within SURFIN_4.2 in transport from Maurer’s clefts to the iRBC surface; and herein we examined if the SURFIN_4.2 intracellular region containing tryptophan-rich (WR) domain is required for its exposure on the iRBC surface.

Results: We generated two transgenic parasite lines which express modified SURFIN_4.2, with or without a part of the intracellular region. Both recombinant SURFIN_4.2 proteins were exported to Maurer’s clefts. However, only SURFIN_4.2 possessing the intracellular region was efficiently cleaved by surface treatment of iRBC with proteinase K.

Conclusions: These results indicate that SURFIN_4.2 is exposed on the iRBC surface and that the intracellular region containing WR domain plays a role on the transport from Maurer’s clefts to the iRBC membrane.