15-Deoxyspergualin modulates Plasmodium falciparum heat shock protein function

Ramya, TNC and Surolia, Namita and Surolia, Avadhesha (2006) 15-Deoxyspergualin modulates Plasmodium falciparum heat shock protein function. In: Biochemical and Biophysical Research Communications, 348 (2). pp. 585-592.

PDF 15-Deoxyspergualin_modulates_Plasmodium_falciparum.pdf Restricted to Registered users only Download (1MB) | Request a copy

Abstract

Heat shock proteins are essential for the survival of all cells. The C-terminal EEVD motif of Hsp70 has previously been implicated in binding 15-deoxyspergualin (DSG), an immunosuppressant with antimalarial activity whose mechanism of action is uncertain. We report the cloning, overexpression, and characterization of three members of the heat shock family, PfHsp70-1 (an Hsp70 protein with a C-terminal EEVD motif), PfHsp70-2 (an Hsp70 protein without the EEVD motif), and PfHsp70 interacting protein. The chaperone activity of PfHsp70-1, and PfHsp70-2 was enhanced by ATP and by PfHip. Interestingly, while binding of protein substrates to PfHsp70-1, PfHsp70-2 and PfHip was unaffected in the presence of DSG, the ATP enhanced chaperone activity of PfHsp70-1 but not PfHsp70-2 was stimulated further by DSG. Our finding suggests that the binding partner of DSG in the parasite cellular milieu is PfHsp70-1 and paves the way for the elucidation of the mechanism of antimalarial action of DSG.

Item Type:	Journal Article
Publication:	Biochemical and Biophysical Research Communications
Publisher:	Elsevier
Additional Information:	Copyright of this article belongs to Elsevier.
Keywords:	Hsp70;Hsp70 interacting protein;Plasmodium falciparum;Chaperone activity;15-Deoxyspergualin
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	27 Nov 2007
Last Modified:	19 Sep 2010 04:32
URI:	http://eprints.iisc.ac.in/id/eprint/8790

Actions (login required)

View Item