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.
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