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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

New observations regarding evolution of trimethoprim resistance.

A clinically isolated strain of Escherichia coli, resistant to more than 1000 mg/l of trimethoprim, expressed chromosomal dihydrofolate reductase to a level 200-fold higher than that of drug sensitive E. coli K-12 strains, and this high cellular enzyme activity was found to increase further when the cells were cultured in the presence of trimethoprim. The induced increase in enzyme activity was dependent on the drug concentration. The increase was six-fold at 100 mg/l of trimethoprim. The aberrantly regulated dihydrofolate reductase gene mediating trimethoprim resistance could be transduced into E. coli K-12 or moved by recombination into an F' factor and then transferred into trans position in relation to the corresponding chromosomal gene. In either of these positions, the synthesis of dihydrofolate reductase could be induced to increase by adding trimethoprim to the culture medium. The observed induction was dependent on protein synthesis, since it could be abolished by chloramphenicol. No other folic acid analogue was found to induce increased expression of the dihydrofolate reductase gene. Also thymine starvation had no effect. Two further clinical isolates of E. coli, highly resistant to trimethoprim, were shown to produce drug resistant, plasmid-mediated dihydrofolate reductases, which were distinct from the earlier known enzyme types I and II.[1]


  1. New observations regarding evolution of trimethoprim resistance. Tennhammar-Ekman, B., Sundström, L., Sköld, O. J. Antimicrob. Chemother. (1986) [Pubmed]
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