Figure 3 | Scientific Reports

Figure 3

From: APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes

Figure 3

IFA of KAHRP-FLAG-APEX2 and biotinylated candidate interactors of KAHRP. (A) 3D7 wild type and KAHRP-FLAG-APEX2 lines incubated with DAPI and anti-FLAG antibodies, followed by detection with Alexa Fluor 555-conjugated anti-mouse antibody. KAHRP-FLAG-APEX2 chimeric protein displayed punctuate localization throughout the parasitized erythrocyte (grey arrows as examples). (B) BP+/H2O2− and BP+/H2O2+ treated KAHRP-FLAG-APEX2 parasites were incubated with DAPI and streptavidin-AF488. As expected, fluorescence, indicating the presence of biotinylated proteins, was observed only in the BP+/H2O2+ treated parasites. (C) BP+/H2O2+ treated KAHRP-FLAG-APEX2 parasites were stained with DAPI, streptavidin-AF488 and anti-MAHRP antibody followed by detection with Alexa-Fluor 546-conjugated anti-rabbit IgG donkey antibody. A clear co-localization between biotinylated proteins (green) and MAHRP (purple) was observed, suggesting that KAHRP interacting partners and MAHRP share the same vesicular compartment in the Maurer’s clefts (merge, white arrows as examples).

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