Abstract
Six Hsp70-like genes are represented on the genome of Plasmodium falciparum. Of these two occur in the cytosol: P. falciparum Hsp70-z (PfHsp70-z) and PfHsp70-1. PfHsp70-1 is a well characterised canonical Hsp70 that facilitates protein quality control and is crucial for the development of malaria parasites. There is very little known about PfHsp70-z. However, PfHsp70-z is known to be essential and is implicated in suppressing aggregation of asparagine-rich proteins of P. falciparum. In addition, its expression at the clinical stage of malaria correlates with disease prognosis. Based on structural evidence PfHsp70-z belongs to the Hsp110 family of proteins. Since Hsp110 proteins have been described as nucleotide exchange factors (NEFs) of their canonical Hsp70 counterparts, it has been speculated that PfHsp70-z may serve as a NEF of PfHsp70-1. In the current study, P. falciparum cells cultured in vitro were subjected to heat stress, triggering the enhanced expression of PfHsp70-z. Biochemical assays conducted using recombinant PfHsp70-z protein demonstrated that the protein is heat stable and possesses ATPase activity. Furthermore, we observed that PfHsp70-z is capable of self-association. The structural-functional features of PfHsp70-z provide further evidence for its role as a chaperone and possible nucleotide exchange factor of PfHsp70-1.
Highlights
An understanding of the biology of the deadly malaria parasite, Plasmodium falciparum, is essential for the development of new therapeutic options in light of the increasing incidences of antimalarial drug resistance
Chloroquine resistance in P. falciparum is mapped to a 36 kb segment of Chromosome 7, which includes the PfHsp70-z (PfCg4) gene [27]
Hsp110-Hsp70 complexes have been implicated in cell division where they modulate the activity of the molecules kenesin-5 motor and cin8, which are required for spindle elongation in yeast and mammalian cells [28]
Summary
An understanding of the biology of the deadly malaria parasite, Plasmodium falciparum, is essential for the development of new therapeutic options in light of the increasing incidences of antimalarial drug resistance. The role of molecular chaperones, amongst them, heat shock proteins (Hsps) in the development of malaria parasites has been well documented [1][2][3]. Hsps play an important house-keeping role in the cell by facilitating protein folding and maintaining. Characterization of the Plasmodium falciparum Hsp70-z (PfHsp70-z) fellowship awarded by the Alexander von Humboldt Foundation, Germany. The South African Research Chairs Initiative of the Department of Science and Technology and National Research Foundation (grant 64788 to HWD) which partially facilitated the study. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript
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