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 L (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 https://doi.org/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 18 - View on Scopus
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