The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum

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Shonhai, A, Boshoff, Aileen and Blatch, Gregory ORCID: 0000-0003-0778-8577 (2007) The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum. Protein Science, 16 (9). pp. 1803-1818. ISSN 0961-8368


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.

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Online ISSN: 1469-896X

Item type Article
DOI 10.1110/ps.072918107
Official URL
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1101 Medical Biochemistry and Metabolomics
Keywords ResPubID22206. PfHsp70, heat shock proteins, Hsp40, molecular chaperones, malaria, Plasmodium falciparum, P. falciparum, DNA, genetics
Citations in Scopus 104 - View on Scopus
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