The export of KAHRP and SBP1 in the PTEX150Δ125-HA mutant compared to full length PTEX150-HA parasites. PTEX150-HA and PTEX150Δ125-HA parasites were synchronized to an invasion window of 5 h. The regions occupied by the parasite are indicated by DAPI and EXP2 staining. KAHRP is a PEXEL protein, which initially displays a diffuse staining of the erythrocyte cytosol before accumulating in punctate regions below the plasma membrane of the host cell. SBP is a PNEP that localizes to punctate vesicular structures called Maurer’s clefts (MC) in the host cytosol. IFAs were counterstained with antibodies to EXP2 to delineate where the boundaries of the parasite. No significant difference between the PTEX150Δ125-HA and PTEX150-HA parasite lines was observed.
Elsworth B, Sanders PR, Nebl T, Batinovic S, Kalanon M, Nie CQ, Charnaud SC, Bullen HE, de Koning Ward TF, Tilley L, Crabb BS, Gilson PR. Proteomic analysis reveals novel proteins associated with the Plasmodium protein exporter PTEX and a loss of complex stability upon truncation of the core PTEX component, PTEX150. Cell Microbiol. 2016 18(11):1551-1569.
Other associated proteins
|PF3D7_0202000||knob-associated histidine-rich protein|
|PF3D7_0501300||skeleton-binding protein 1|
|PF3D7_1471100||exported protein 2|