PfHsp70-x interacts with exported Hsp40s and PfEMP1. A. proximity ligation assay (PLA) of (upper panel) PfHsp70-x/PfEMP1, (second panel) PfHsp70-x/A660-GFP (PFA0660w), (third panel) PfHsp70-x/E55-GFP (PFE0055c). A red signal indicates a positive interaction. Lower panel shows negative control. PfHsp70-x appears to closely interact with the ATS of PfEMP1, and both exported Hsp40s studied.Külzer S, Charnaud S, Dagan T, Riedel J, Mandal P, Pesce ER, Blatch GL, Crabb BS, Gilson PR, Przyborski JM. Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte. Cell Microbiol. 2012 14(11):1784-95

Parasites were tagged by single cross-over homologous recombination, the endogenous gene locus to include the GFP coding sequence. PFA660INT. Co-immunofluorescence analysis on erythrocytes infected with PFA660INT, using anti-sera directed against STEVOR (A), MAHRP1 MAL13P1.413 (B), KAHRP PFB0100c (C). Fluorescence channels are shown individually in black/white for highest contrast. All images are maximal projections of Z-stack serial sections. In merge image green, GFP; red, STEVOR (A), MAHRP (B), KAHRP (C) or ATS domain of PfEMP1 (D); blue, Hoechst. Inset shows enlargement of merge (white box). The fusion protein labelled punctate structures within the infected erythrocytebut clearly not in Maurer’s clefts.Külzer S, Rug M, Brinkmann K, Cannon P, Cowman A, Lingelbach K, Blatch GL, Maier AG, Przyborski JM. Parasite encoded Hsp40 proteins define novel mobile structures in the cytosol of the P. falciparum infected erythrocyte. Cell Microbiol. 2010 12(10):1398-420. Copyright John Wiley & Sons Ltd. 2010.