Abstract
Malaria is still one of the major killer parasitic diseases in tropical settings, posing a public health threat. The development of antimalarial drug resistance is reversing the gains made in attempts to control the disease. The parasite leads a complex life cycle that has adapted to outwit almost all known antimalarial drugs to date, including the first line of treatment, artesunate. There is a high unmet need to develop new strategies and identify novel therapeutics to reverse antimalarial drug resistance development. Among the strategies, here we focus and discuss the merits of the development of antimalarials targeting the Heat shock protein 90 (Hsp90) due to the central role it plays in protein quality control.
Highlights
Malaria still poses a major public health burden globally, with an estimated 229 million cases and more than 419,000 deaths; most of these deaths being in the tropics in the year2019 [1]
When geldanamycin was first identified as a potent Heat shock protein 90 (Hsp90) inhibitor, its derivatization soon ensued, and many more Hsp90 inhibitors were developed
These efforts were mainly driven by the essential role that Hsp90 plays in eukaryotes and its implication in various diseases, such as numerous cancers and parasitic diseases [185,186]
Summary
Malaria still poses a major public health burden globally, with an estimated 229 million cases and more than 419,000 deaths; most of these deaths being in the tropics in the year. Sub-Saharan Africa accounts for about 95% of all malarial deaths, and of these, 67%. Are children under the age of 5 years [1]. The protozoan parasite responsible for malaria in humans are the single-celled eukaryote Plasmodium species in the phylum Apicomplexa. P. falciparum is responsible for the deadliest form of the disease in humans [2]. Efforts to eradicate malaria have been limited due to the complex life cycle of the parasite and the absence of an effective vaccine. Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations
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