Localisation and expression of PfHop-GFP by parasites in human red blood cells. a Localisation of PfHop in P. falciparum cells; panels show a DIC image, nuclear stain (Hoechst), distribution of PfHop, merge and overlay. b Panels show a DIC image, nuclear stain (Hoechst), distribution of PfHop-GFP, merge and overlay. c Panels show a DIC image, nucleus (Hoechst), distribution of PfHop-GFP, distribution of PfHsp90, merge and overlay for PfHsp90–PfHop-GFP co-localisation. d Panels show DIC image, stain (Hoechst), distribution of PfHop-GFP, distribution of PfHsp70, merge and overlay. PfHop displayed a similar cytosolic localisation profile to PfHsp90 (b), suggesting that the two proteins may associate. Although, PfHop-GFP and PfHsp70 exhibited overlapping cytosolic co-localisation signals, the PfHsp90–PfHop-GFP co-localisation signal was more uniform than that for PfHsp70–PfHop-GFP (b, c). It is possible that PfHop associates more closely with PfHsp90 than with PfHsp70. Gitau GW, Mandal P, Blatch GL, Przyborski J, Shonhai A. Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop). Cell Stress Chaperones. 2011 17(2):191-202.

Immunofluorescence staining to detect Hsp40, HSP70, HSP90 and HOP was conducted on trophozoite stage P. falciparum-infected erythrocytes. Panels show from left to right a DIC image, distribution of protein of interest (POI), nuclear stain (Hoechst), merge and overlay (localization relative to the parasite nucleus and phase-contrast image). All proteins showed cytosolic localization.Botha M, Chiang AN, Needham PG, Stephens LL, Hoppe HC, Külzer S, Przyborski JM, Lingelbach K, Wipf P, Brodsky JL, Shonhai A, Blatch GL. Plasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shock. Cell Stress Chaperones. 2011 16(4):389-401. Pictures were kindly provided by Jude Przyborski.