The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns

Full text for this resource is not available from the Research Repository.

Pesce, Eva-Rachele , Acharya, P, Tatu, U, Nicoll, W, Shonhai, A, Hoppe, H and Blatch, Gregory L (2008) The Plasmodium falciparum heat shock protein 40, Pfj4, associates with heat shock protein 70 and shows similar heat induction and localisation patterns. International Journal of Biochemistry and Cell Biology, 40 (12). pp. 2914-2926. ISSN 1357-2725

Abstract

Human cerebral malaria is caused by the protozoan parasite Plasmodium falciparum, which establishes itself within erythrocytes. The normal body temperature in the human host could constitute a possible source of heat stress to the parasite. Molecular chaperones belonging to the heat shock protein (Hsp) class are thought to be important for parasite subsistence in the host cell, as the expression of some members of this family has been reported to increase upon heat shock. In this paper we investigated the possible functions of the P. falciparum heat shock protein DnaJ homologue Pfj4, a type II Hsp40 protein. We analysed the ability of Pfj4 to functionally replace Escherichia coli Hsp40 proteins in a dnaJ cbpA mutant strain. Western analysis on cellular fractions of P. falciparum-infected erythrocytes revealed that Pfj4 expression increased upon heat shock. Localisation studies using immunofluorescence and immuno-electron microscopy suggested that Pfj4 and P. falciparum Hsp70, PfHsp70-1, were both localised to the parasites nucleus and cytoplasm. In some cases, Pfj4 was also detected in the erythrocyte cytoplasm of infected erythrocytes. Immunoprecipitation studies and size exclusion chromatography indicated that Pfj4 and PfHsp70-1 may directly or indirectly interact. Our results suggest a possible involvement of Pfj4 together with PfHsp70-1 in cytoprotection, and therefore, parasite survival inside the erythrocyte.

Dimensions Badge

Altmetric Badge

Additional Information

Online ISSN: 1878-5875

Item type Article
URI https://vuir.vu.edu.au/id/eprint/8148
DOI https://doi.org/10.1016/j.biocel.2008.06.011
Official URL http://dx.doi.org/10.1016/j.biocel.2008.06.011
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1108 Medical Microbiology
Keywords ResPubID22202. heat shock proteins, Hsp40, DNA, malaria, complementation
Citations in Scopus 48 - View on Scopus
Download/View statistics View download statistics for this item

Search Google Scholar

Repository staff login