Co-expression of the Plasmodium falciparum chaperone, PfHsp70, improves the heterologous production of the antimalarial drug target GTP cyclohydrolase I, PfGCHI

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Stephens, Linda L, Shonhai, Addmore and Blatch, Gregory ORCID: 0000-0003-0778-8577 (2011) Co-expression of the Plasmodium falciparum chaperone, PfHsp70, improves the heterologous production of the antimalarial drug target GTP cyclohydrolase I, PfGCHI. Protein Expression and Purification, 77 (2). pp. 159-165. ISSN 1046-5928

Abstract

Folates are ubiquitous in rapidly dividing cells as found in the malaria parasite and little is known about the folate pathway in Plasmodium compared to the same pathway in the human host. The co-expression of the molecular chaperone, PfHsp70 with PfGCHI improved the production of the latter in E. coli. The fact that PfGCHI was produced as soluble and active protein is of importance towards its characterisation as a potential antimalarial drug target. A putative structure for PfGCHI would greatly aid the design of drugs specific to PfGCHI.

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Item type	Article
URI	https://vuir.vu.edu.au/id/eprint/9021
DOI	10.1016/j.pep.2011.01.005
Official URL	http://dx.doi.org/10.1016/j.pep.2011.01.005
Subjects	Historical > Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences Historical > FOR Classification > 0601 Biochemistry and Cell Biology Historical > SEO Classification > 970111 Expanding Knowledge in the Medical and Health Sciences
Keywords	ResPubID23323, co-expression, protein folding, heat shock proteins, Hsp70, molecular chaperone, plasmodium falciparum
Citations in Scopus	20 - View on Scopus
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