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Mycoplasma pneumoniae thymidine phosphorylase.

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  • 1a Department of Anatomy, Physiology and Biochemistry , Swedish University of Agricultural Sciences, The Biomedical Center , Uppsala , Sweden.

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Mycoplasma pneumoniae lacking thymidine phosphorylase (TP) showed altered nucleoside metabolism and enzyme activity. This suggests targeting Mycoplasma nucleotide biosynthesis enzymes could lead to new antibiotic development.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Drug Discovery

Background:

  • Mycoplasma pneumoniae causes respiratory infections and impacts anticancer/antiviral drug efficacy.
  • Mycoplasma thymidine phosphorylase (TP) interferes with nucleoside analog drugs.

Purpose of the Study:

  • To investigate the role of M. pneumoniae TP in nucleoside analog metabolism.
  • To generate a TP-deficient M. pneumoniae strain for studying drug interactions.

Main Methods:

  • Generated a TP-deficient M. pneumoniae mutant.
  • Assessed radiolabeled deoxyuridine, uracil, and thymidine uptake.
  • Screened 30 FDA-approved nucleoside/nucleobase analogs for growth inhibition.

Main Results:

  • TP deficiency increased deoxyuridine and uracil uptake, with upregulated salvage enzymes.
  • Thymidine uptake remained unaffected in the TP-deficient strain.
  • Seven analogs inhibited both wild-type and TP-deficient M. pneumoniae growth; purine analogs showed strain-specific effects.

Conclusions:

  • TP is not essential for M. pneumoniae survival.
  • TP deficiency impacts nucleotide metabolism and salvage pathways.
  • Mycoplasma nucleotide biosynthesis enzymes are potential antibiotic targets.