The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum

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

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Official URL: http://dx.doi.org/10.1110/ps.072918107

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:Research article
Uncontrolled Keywords:Heat shock protein; Hsp40; Malaria; Molecular chaperone; PfHsp70; heat shock protein 40; heat shock protein 70; nuclear protein; protein expression; protein function; protein phosphorylation; protein structure; HSP70 Heat-Shock Proteins; Protozoan Proteins
Subjects:Y Unknown > Subjects to be assigned
Divisions:Faculty > Faculty of Science > Biochemistry, Microbiology & Biotechnology
ID Code:1396
Deposited By: Mrs Eileen Shepherd
Deposited On:29 Jun 2009
Last Modified:06 Jan 2012 16:20
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