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Genetic characterization of trimethoprim resistance in Haemophilus influenzae

R de Groot1, M Sluijter, A de Bruyn

  • 1Department of Pediatrics, Sophia Children's Hospital, Erasmus University Rotterdam, The Netherlands.

Insights

Trimethoprim resistance in Haemophilus influenzae is linked to changes in dihydrofolate reductase (DHFR). Alterations in the DHFR gene

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Trimethoprim (Tmp) resistance in Haemophilus influenzae is primarily mediated by chromosomally encoded dihydrofolate reductase (DHFR) with altered structure and kinetics.
  • Understanding the structure-function relationship of DHFR is crucial for comprehending Tmp resistance mechanisms.

Purpose of the Study:

  • To investigate the relationship between dihydrofolate reductase (DHFR) gene structure and the level of trimethoprim (Tmp) resistance in Haemophilus influenzae.
  • To characterize the folH genes from Tmp-susceptible and Tmp-resistant H. influenzae strains.

Main Methods:

  • Cloning and characterization of folH genes from susceptible and resistant H. influenzae strains.
  • Construction and analysis of folH gene hybrids in Escherichia coli to assess Tmp susceptibility.
  • Investigating the impact of promoter and coding sequence variations on Tmp resistance.

Main Results:

  • Differences in promoter regions and coding sequences of folH genes were observed between susceptible and resistant H. influenzae isolates.
  • In E. coli, resistance mediated by H. influenzae folH (R1047) involved promoter and central folH alterations.
  • Resistance mediated by H. influenzae folH (R1042) in E. coli was linked to alterations in C-terminal amino acid residues.

Conclusions:

  • Trimethoprim resistance is associated with modifications beyond the promoter and N-terminal/central Tmp binding domains of DHFR.
  • Alterations in the C-terminal region of DHFR can contribute to Tmp resistance, likely by affecting secondary structure and Tmp binding affinity.
  • These findings expand the understanding of molecular mechanisms underlying trimethoprim resistance in H. influenzae.

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