Host Chaperones Are Recruited in Membrane-bound Complexes by Plasmodium falciparum

Banumathy, Gowrishankar and Singh, Varsha and Tatu, Utpal (2002) Host Chaperones Are Recruited in Membrane-bound Complexes by Plasmodium falciparum. In: The Journal of Biological Chemistry, 277 (6). pp. 3902-3912.

PDF Host_Chaperones.pdf - Published Version Restricted to Registered users only Download (569kB) | Request a copy

Abstract

The ability of malarial parasite to deploy proteins at the surface of infected erythrocytes is well known. After their synthesis within the parasite, the cargo proteins are exported from the parasite and carried across the erythrocyte cytoplasm to be delivered at the erythrocyte surface. Our knowledge about the mechanisms involved in this complex trafficking path is limited. We have addressed the involvement of chaperones in traffic across erythrocyte cytoplasm. Our analyses of the chaperones available to the parasite indicated that none of the reported chaperones of the parasite origin are present in the erythrocyte cytoplasm. The chaperones of the host (Hsp70, Hsp90, Hop60), on the other hand, were readily detected in the erythrocyte cytosol. Hypotonic lysis and detergent solubilization experiments indicated that unlike their soluble nature in normal erythrocytes, host chaperones are recruited in membrane-bound, detergent-resistant complexes in infected cells. The association of host-Hsp70 with detergent-resistant complexes was ATP-dependent. Importantly, host chaperones could be detected in knob-enriched fractions and could be cross-linked to the knob subunit, PfHRP1, in a large complex at the surface of the infected erythrocytes. Our results implicate host chaperones in the assembly of parasite proteins such as knob subunits at the erythrocyte surface.

Item Type:	Journal Article
Publication:	The Journal of Biological Chemistry
Publisher:	The American Society for Biochemistry and Molecular Biology
Additional Information:	Copyright of this article belongs to The American Society for Biochemistry and Molecular Biology.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	06 Jul 2007
Last Modified:	24 Jan 2012 07:18
URI:	http://eprints.iisc.ac.in/id/eprint/11431

Actions (login required)

View Item