Heat shock protein 90 (Hsp90), an ATP-dependent molecular chaperone, is a highly conserved and
ubiquitously expressed stress protein in eukaryotes. It is responsible for activation of various proteins involved in signal
transduction, cell cycle control, hormone signaling, and transcription. Anomalous expression of this family can be
associated with several disease states. Current article focuses on the novel use of Hsp90 inhibitors as antimalarial agents.
The present armamentarium of antimalarial therapy is not proving itself as an adequate treatment to eradicate malaria
completely. This inadequacy is mainly due to the increasing drug resistance rate in Plasmodium species. The parasite
Plasmodium falciparum requires Hsp90 (Pfhsp90) for regulating its development. Analysis of PfHsp90 function suggests
that it regulates parasite development during the frequent febrile episodes that are characteristic of malaria. This crucial
role of Hsp90 in the growth and development of the parasite has attracted many researchers as a potential target for
malaria and other infectious diseases. Currently there are about seven antimalarial and more than thirty anticancer Hsp90
inhibitors in various phases of drug development. Addition of alternatives with novel mechanism to the current treatment
armoury may eventually help improve the outcomes of malaria. It is prudent to remain optimistic as the research in this
field continues to evolve.
Keywords: Heat shock protein, Hsp90, Hsp90 inhibitors, Plasmodium falciparum, PfHsp90, malaria.
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Published on: 09 October, 2013
Page: [1903 - 1920]