Research Repository

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

Stephens, Linda L and 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

Full text for this resource is not available from the Research Repository.

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.

Item Type: Article
Uncontrolled Keywords: ResPubID23323, co-expression, protein folding, heat shock proteins, Hsp70, molecular chaperone, plasmodium falciparum
Subjects: Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
FOR Classification > 0601 Biochemistry and Cell Biology
SEO Classification > 970111 Expanding Knowledge in the Medical and Health Sciences
Depositing User: VUIR
Date Deposited: 08 Aug 2012 02:05
Last Modified: 08 Aug 2012 02:05
URI: http://vuir.vu.edu.au/id/eprint/9021
DOI: 10.1016/j.pep.2011.01.005
ePrint Statistics: View download statistics for this item
Citations in Scopus: 5 - View on Scopus

Repository staff only

View Item View Item

Search Google Scholar