Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop)

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Gitau, Grace W, Mandal, Pradipta, Blatch, Gregory ORCID: 0000-0003-0778-8577, Przyborski, Jude M and Shonhai, Addmore (2012) Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop). Cell Stress and Chaperones, 17 (2). pp. 191-202. ISSN 1355-8145


Malaria is caused by Plasmodium species, whose transmission to vertebrate hosts is facilitated by mosquito vectors. The transition from the cold blooded mosquito vector to the host represents physiological stress to the parasite, and additionally malaria blood stage infection is characterised by intense fever periods. In recent years, it has become clear that heat shock proteins play an essential role during the parasite's life cycle. Plasmodium falciparum expresses two prominent heat shock proteins: heat shock protein 70 (PfHsp70) and heat shock protein 90 (PfHsp90). Both of these proteins have been implicated in the development and pathogenesis of malaria. In eukaryotes, Hsp70 and Hsp90 proteins are functionally linked by an essential adaptor protein known as the Hsp70–Hsp90 organising protein (Hop). In this study, recombinant P. falciparum Hop (PfHop) was heterologously produced in E. coli and purified by nickel affinity chromatography. Using specific anti-PfHop antisera, the expression and localisation of PfHop in P. falciparum was investigated. PfHop was shown to co-localise with PfHsp70 and PfHsp90 in parasites at the trophozoite stage. Gel filtration and coimmunoprecipitation experiments suggested that PfHop was present in a complex together with PfHsp70 and PfHsp90. The association of PfHop with both PfHsp70 and PfHsp90 suggests that this protein may mediate the functional interaction between the two chaperones.

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Item type Article
DOI 10.1007/s12192-011-0299-x
Official URL
Subjects Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
Historical > FOR Classification > 1108 Medical Microbiology
Keywords ResPubID24899, ResPubID25406, clone, over-expression, purification, heat shock protein, anti-peptide antibodies, parasites, antimalarial drug, malaria, intervention strategies
Citations in Scopus 57 - View on Scopus
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