Publication: Cloning and heterologous expression of Plasmodium ovale dihydrofolate reductase-thymidylate synthase gene
Issued Date
2012-06-01
Resource Type
ISSN
18730329
13835769
13835769
Other identifier(s)
2-s2.0-84857799150
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Parasitology International. Vol.61, No.2 (2012), 324-332
Suggested Citation
Srisuda Tirakarn, Pinpunya Riangrungroj, Palangpon Kongsaeree, Mallika Imwong, Yongyuth Yuthavong, Ubolsree Leartsakulpanich Cloning and heterologous expression of Plasmodium ovale dihydrofolate reductase-thymidylate synthase gene. Parasitology International. Vol.61, No.2 (2012), 324-332. doi:10.1016/j.parint.2011.12.004 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/14313
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Cloning and heterologous expression of Plasmodium ovale dihydrofolate reductase-thymidylate synthase gene
Other Contributor(s)
Abstract
Plasmodial bifunctional dihydrofolate reductase-thymidylate synthase (DHFR-TS) is a validated antimalarial drug target. In this study, expression of the putative dhfr-ts of Plasmodium ovale rescued the DHFR chemical knockout and a TS null bacterial strain, demonstrating its DHFR and TS catalytic functions. PoDHFR-TS was expressed in Escherichia coli BL21 (DE3) and affinity purified by Methotrexate Sepharose column. Biochemical and enzyme kinetics characterizations indicated that PoDHFR-TS is similar to other plasmodial enzymes, albeit with lower catalytic activity but better tolerance of acidic pH. Importantly, the PoDHFR from Thai isolate EU266602 remains sensitive to the antimalarials pyrimethamine and cycloguanil, in contrast to P. falciparum and P. vivax isolates where resistance to these drugs is widespread. © 2011 Elsevier Ireland Ltd.