The C-terminus of PFD0495c functions within the erythrocyte cytoplasm and mediates interactions important for
intraerythrocytic development. (A) Topology of PFD0495c in transgenic clone 1 parasites. C-terminus of PFD0495c-GFP is localized to erythrocyte cytoplasmic face. Anti-GFP signal is detected after tetanolysin permeabilization. Control signal to PPM (aMSP-1) is detected only with saponin treatment. p, parasite; e, erythrocyte; arrow, erythrocyte membrane; arrowhead, intraerythrocytic vesicle/tubule. Asterisk marks neighboring cell. (B) Schematic of selective permeabilization experiment. Tetanolysin selectively permeabilizes only the erythrocyte plasma membrane, leaving the PVM intact. Only in
combination with saponin will the PVM be permeabilized and control MSP1 antibodies gain access to epitope. If anti-GFP signal can be detected with tetanolysin alone, then the C-terminus is present on the cytoplasmic face of the erythrocyte.
Tamez PA, Bhattacharjee S, van Ooij C, Hiller NL, Llinás M, Balu B, Adams JH, Haldar K. An erythrocyte vesicle protein exported by the malaria parasite promotes tubovesicular lipid import from the host cell surface. PLoS Pathog. 2008 Aug 8;4(8):e1000118.
Other associated proteins
|PF3D7_0930300||merozoite surface protein 1|