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No stress – Hsp90 and signal transduction in Leishmania

Published online by Cambridge University Press:  04 April 2014

A. HOMBACH  and
J. CLOS
A. HOMBACH
Affiliation:
Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht St. 74, 20359 Hamburg, Germany
J. CLOS*
Affiliation:
Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht St. 74, 20359 Hamburg, Germany
*
*Corresponding author:Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht St 74, 20359 Hamburg, Germany. E-mail: clos@bnitm.de
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Summary

Hsp90 (a.k.a. Hsp83) plays a significant role in the life cycle control of the protozoan parasite Leishmania donovani. Rather than protecting Leishmania spp. against adverse and stressful environs, Hsp90 is required for the maintenance of the motile, highly proliferative insect stage, the promastigote. However, Hsp90 is also essential for survival and proliferation of the intracellular mammalian stage, the amastigote. Moreover, recent evidence shows Hsp90 and other components of large multi-chaperone complexes as substrates of stage-specific protein phosphorylation pathways, and thus as likely effectors of the signal transduction pathways in Leishmania spp. Future efforts should be directed towards the identification of the protein kinases and the critical phosphorylation sites as targets for novel therapeutic approaches.

Keywords

LeishmaniaHsp90heat shocksignal transductionradicicol
Type
Special Issue Article
Information
Parasitology , Volume 141 , Special Issue 9: Heat shock proteins as drug targets in infectious diseases , August 2014 , pp. 1156 - 1166
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Copyright
Copyright © Cambridge University Press 2014 

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