Volume 9 Supplement 2
Identification and characterization of novel Plasmodium falciparum cyclophilins and their roles in the antimalarial actions of cyclosporin A and derivatives
© Marin-Menendez and Bell; licensee BioMed Central Ltd. 2010
Published: 20 October 2010
Results and conclusions
All but three of the cyclophilin/cyclophilin-like genes (or in the case of the larger proteins, their CYP domains) were cloned identically into a pET vector encoding a C-terminal His6-tag and eight of them were successfully expressed in Escherichia coli and purified using nickel-chelate affinity chromatography. All of the recombinant proteins showed chaperone activity on model substrates, while only PfCYP19A and PfCYP19B demonstrated peptidyl-prolyl isomerase (foldase) activity and were bound by CsA. Our data suggest the existence of a cyclophilin-type chaperone family whose partner proteins are not yet known but might include proteins exported to the host erythrocyte.
This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.