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Cloning and heterologous expression of Plasmodium ovale dihydrofolate reductase-thymidylate synthase gene.

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.

journal_name

Parasitol Int

journal_title

Parasitology international

authors

Tirakarn S,Riangrungroj P,Kongsaeree P,Imwong M,Yuthavong Y,Leartsakulpanich U

doi

10.1016/j.parint.2011.12.004

subject

Has Abstract

pub_date

2012-06-01 00:00:00

pages

324-32

issue

2

eissn

1383-5769

issn

1873-0329

pii

S1383-5769(11)00207-8

journal_volume

61

pub_type

杂志文章

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