Journal
FEMS MICROBIOLOGY LETTERS
Volume 256, Issue 1, Pages 105-111Publisher
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2005.00095.x
Keywords
Plasmodium vivax; dihydrofolate reductase (DHFR); sulphanilamide; sulpha-dihydropteroate (sulpha-DHP); antifolate; folate biosynthesis
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Sulpha drugs act as competitive inhibitors of p-amino benzoic acid, an intermediate in the de novo folate pathway. Dihydropteroate synthase condenses sulpha drugs into sulpha-dihydropteroate (sulpha-DHP), which competes with dihydrofolate, the dihydrofolate reductase (DHFR) substrate. This designates DHFR as a possible target of sulpha-DHP. We suggest here that Plasmodium vivax DHFR is indeed the in vivo target of sulpha drugs. The wild-type DHFR expressed in Saccharomyces cerevisiae leads to cell growth inhibition, while sensitivity to the drug is exacerbated in the mutants. Contrary to what is observed with sulphanilamide, methotrexate is less effective on P. vivax-DHFR mutants than on wild-type mutant.
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