Elucidating the Molecular Mechanism(s) Underlying the Subcellular Distribution of PF3D7_0410600 Protein in the Malaria Parasite

Abstract

Malaria still poses a global threat despite the enormous research and intervention strategies that have been employed to curb the menace of the disease over the years. This has necessitated the characterization of novel drug targets for the development of new intervention against malaria. In this study, I identified two novel P. falciparum proteins (PF3D7_0410600 and PF3D7_1459400) and used cellular/biochemical approaches to characterize the proteins. Analysis of the protein sequences revealed structural features that present the novel proteins as key players during the malaria parasite development. I generated rabbit antibodies against the two novel proteins and showed detection of the native parasite proteins in immunoblotting and immunofluorescence assays. The results suggest that PF3D7_1459400 protein may be exported and possibly associates with parasite-induced structures. I also observed that PF3D7_0410600 protein which overlapped with a component of the inner membrane complex (IMC), may not be palmitoylated and only geranylgeranyl transferase inhibitor (GGTI) seemed to have impacted on the localization of the protein. My analysis also suggests that protein-protein interactions may be the probable molecular mechanism governing the recruitment of PF3D7_0410600 protein to the periphery of the parasite. It is therefore conceivable that disruption of the IMC-microtubular interplay may alter the parasite morphology, which may consequently affect its survival, and hence present PF3D7_0410600 protein as a suitable target for such a drug development approach. Similarly, the functional investigation of PF3D7_0410600 protein and its associated complex may provide further understanding on the fascinating biology of the malaria parasite