15-Deoxyspergualin modulates Plasmodium falciparum heat shock protein function

Ramya, T. N. C. ; Surolia, Namita ; Surolia, Avadhesha (2006) 15-Deoxyspergualin modulates Plasmodium falciparum heat shock protein function Biochemical and Biophysical Research Communications, 348 (2). pp. 585-592. ISSN 0006-291X

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.bbrc.2006.07.082

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:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Hsp70; Hsp70 Interacting Protein; Plasmodium falciparum; Chaperone Activity; 15-Deoxyspergualin
ID Code:75562
Deposited On:24 Dec 2011 11:46
Last Modified:03 Jul 2012 05:52

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