PF3D7_0202000 knob-associated histidine-rich protein

PMV disruption reduces expression of the exported protein HRP2. IFA of schizonts of control (DMSO-treated) and RAP-treated integrant clone PMV-C5 ~42 h following treatment (cycle 0). Upon RAP-treatment, site specific recombination between the introduced loxP sites in the modified pfpmv locus of the PMV-C5 parasites was anticipated to reconstitute a single functional loxP-containing intron. Splicing of this intron results in a truncated form of PMV lacking the HA epitope tag, as well as allowing expression of free GFPץ The PMV-HA signal was lost following RAP treatment. Localization of MSP1, KAHRP and HRP2 was unaffected; however, the HRP2 signal was significantly decreased in intensity. Parasite nuclei were visualised by staining with DAPI. Scale bars, 5 μm. Results shown are typical of two separate experiments. The localization and intensity of the MSP1 signal and the KHARP signal did not alter upon RAP-treatment, correlating well with the western blot analysis. The HRP2 signal remained detectable in both control and the RAP-treated parasites, but in contrast to the other proteins examined, the fluorescence intensity of the HRP2 signal was substantially decreased in RAP-treated parasites, suggesting a partial effect of PMV depletion on HRP2 trafficking

Boonyalai N, Collins CR, Hackett F, Withers-Martinez C, Blackman MJ. Essentiality of Plasmodium falciparum plasmepsin V. PLoS One. 2018 13(12):e0207621

Other associated proteins

PFID Formal Annotation
PF3D7_0831800 histidine-rich protein II
PF3D7_0930300 merozoite surface protein 1
PF3D7_1323500 PEXEL protease plasmepsin V