Research Repository

The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum

Shonhai, A and Boshoff, A and Blatch, Gregory L (2007) The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum. Protein Science, 16 (9). pp. 1803-1818. ISSN 0961-8368

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

Abstract

It is becoming increasingly apparent that heat shock proteins play an important role in the survival of Plasmodium falciparum against temperature changes associated with its passage from the cold-blooded mosquito vector to the warm-blooded human host. Interest in understanding the possible role of P. falciparum Hsp70s in the life cycle of the parasite has led to the identification of six HSP70 genes. Although most research attention has focused primarily on one of the cytosolic Hsp70s (PfHsp70-1) and its endoplasmic reticulum homolog (PfHsp70-2), further functional insights could be inferred from the structural motifs exhibited by the rest of the Hsp70 family members of P. falciparum. There is increasing evidence that suggests that PfHsp70-1 could play an important role in the life cycle of P. falciparum both as a chaperone and immunogen. In addition, P. falciparum Hsp70s and Hsp40 partners are implicated in the intracellular and extracellular trafficking of proteins. This review summarizes data emerging from studies on the chaperone role of P. falciparum Hsp70s, taking advantage of inferences gleaned from their structures and information on their cellular localization. The possible associations between P. falciparum Hsp70s with their cochaperone partners as well as other chaperones and proteins are discussed.

Item Type: Article
Additional Information:

Online ISSN: 1469-896X

Uncontrolled Keywords: ResPubID22206. PfHsp70, heat shock proteins, Hsp40, molecular chaperones, malaria, Plasmodium falciparum, P. falciparum, DNA, genetics
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 1101 Medical Biochemistry and Metabolomics
Depositing User: VUIR
Date Deposited: 03 Apr 2012 23:31
Last Modified: 03 Apr 2012 23:31
URI: http://vuir.vu.edu.au/id/eprint/8151
DOI: 10.1110/ps.072918107
ePrint Statistics: View download statistics for this item
Citations in Scopus: 37 - View on Scopus

Repository staff only

View Item View Item

Search Google Scholar