Trimethoprim Action and Its Analogy with Thymine Starvation

Author:

Amyes S. G. B.1,Smith J. T.1

Affiliation:

1. Department of Pharmaceutics, The School of Pharmacy, University of London, Brunswick Square, London, WC1N 1AX, United Kingdom

Abstract

In a minimal medium, trimethoprim is merely bacteriostatic on the prototroph Escherichia coli 114. The drug was bactericidal when the amino acids methionine and glycine, plus a purine or purine nucleoside, were also present. This response could be reversed completely when thymine and lysine were added to the culture. Methionine, glycine, and the purine are thought to maintain the integrity of the tetrahydrofolate pool under trimethoprim treatment and prevent the thymidylate synthetase reaction. Thus, the organism behaves phenotypically as a thymineless mutant. The mechanisms by which thymine and lysine reverse the bactericidal effect of trimethoprim in a minimal medium containing methionine, glycine, and adenine is discussed.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference36 articles.

1. Nature of trimethopriminduced death in Escherichia coli;Angehrn P.;Arnzeimittel-Forsch.,1973

2. The induction of thymine synthesis by T2 infection of a thymine requiring mutant of Escherichia coli;Barner H. D.;J. Bacteriol.,1954

3. Virus-induced acquisition of metabolic function. IV. Thymidylate synthetase in thymine-requiring Escherichia coli infected by T, and T4 bacteriophages;Barner H. D.;J. Biol. Chem.,1959

4. Constitutivity of thymidine phosphorylase in deoxyriboaldolase negative strains: dependence on thymine requirement;Beacham I. R.;Biochim. Biophys. Acta,1968

5. The role of nucleoside phosphorylase in the degradation of deoxyribonucleosides by thymine-requiring mutants of E. coli;Beacham I. R.;Mol. Gen. Genet.,1971

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