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Biological Characterization of Plasmodium falciparum Mitochondrial Heat Shock Protein PfHsp70-3: Possible Involvement in Malaria Pathogenesis

Authors :
David Onchonga Nyakundi
Aileen Boshoff
Source :
Tanzania Journal of Science; Vol. 47 No. 4 (2021); 1338-1351
Publication Year :
2021
Publisher :
College of Natural and Applied Sciences (CoNAS) of the University of Dar es Salaam (UDSM), 2021.

Abstract

Malaria remains a global health burden accounting for many deaths and illnesses in sub-Saharan Africa notwithstanding many decades of research on the disease. P. falciparum, the causative agent of the most fatal form of malaria, expresses a repertoire of heat shock proteins (Hsp) that cushion the parasite against heat shocks as it shuttles between extreme temperatures in human and mosquito vector hosts. By so doing, such proteins promote parasite’s cytoprotection, survival and pathogenesis. Heat shock proteins are named according to their molecular weights and there are six P. falciparum Hsp70 (PfHsp70) found in various cell compartments with mitochondrial putative PfHsp70-3. Using indirect immunofluorescence, this study established mitochondrial localization of PfHsp70-3 though some more confirmatory studies would be needed in the future. PfHsp70-3 was found to be heat inducible and expressed during all stages of the intra-erythrocytic cycle of parasite development. This could be an indication of PfHsp70-3’s involvement in the infectivity process of P. falciparum by helping the parasite to resist heat shocks during malaria febrile episodes. Generally, the data obtained in this study will enhance the existing knowledge on the biology of P. falciparum mitochondrial heat shock protein functions and open possible avenues for targeting the specificity between PfHsp70-3 and its co-chaperones for drug development. Keywords: Malaria, P. falciparum, Heat shock proteins, PfHsp70-3, pathogenesis

Details

Language :
English
ISSN :
08561761 and 25077961
Database :
OpenAIRE
Journal :
Tanzania Journal of Science
Accession number :
edsair.doi.dedup.....237b626bbb98e46bb332dddc2706fd36