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Effect of temperature on aminoglycoside binding sites in Stenotrophomonas maltophilia

A Rahmati-Bahram1, J T Magee, S K Jackson

  • 1Department of Medical Microbiology, University of Wales College of Medicine, Cardiff, UK.

Insights

Temperature affects Stenotrophomonas maltophilia sensitivity to gentamicin, with lipopolysaccharide (LPS) phosphate content playing a key role. Higher LPS phosphate at 37°C increases gentamicin susceptibility in some strains.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Stenotrophomonas maltophilia exhibits temperature-dependent variations in sensitivity (TDVS) to gentamicin.
  • Lipopolysaccharide (LPS) is a key component of the Gram-negative bacterial outer membrane and can influence antibiotic resistance.
  • Understanding the molecular basis of TDVS is crucial for developing effective antimicrobial strategies.

Purpose of the Study:

  • To investigate the role of lipopolysaccharide (LPS) in temperature-dependent variations in sensitivity (TDVS) to gentamicin in Stenotrophomonas maltophilia.
  • To determine if changes in LPS composition, specifically phosphate and KDO content, correlate with TDVS.
  • To elucidate the interaction site of gentamicin with LPS.

Main Methods:

  • Culturing S. maltophilia strains at 30°C and 37°C.
  • Quantifying LPS phosphate and 3-deoxy-D-manno-octulosonic acid (KDO) content.
  • Assessing gentamicin sensitivity using minimum inhibitory concentration (MIC) determination.
  • Analyzing gentamicin binding to bacterial cells using fluorescence-activated cell sorting (FACS).

Main Results:

  • Strains with 'good' TDVS showed significantly higher LPS phosphate content at 37°C compared to 30°C (P < 0.001).
  • Strains with 'poor' TDVS did not exhibit significant changes in LPS phosphate content with temperature.
  • No significant difference in KDO content was observed between temperatures for either group.
  • FACS analysis revealed temperature-dependent differences in gentamicin binding to bacterial cells.

Conclusions:

  • Temperature-dependent variation in aminoglycoside susceptibility in S. maltophilia is strongly correlated with LPS phosphate content.
  • LPS phosphate, not KDO, is the primary site for ionic interactions with aminoglycosides like gentamicin.
  • These findings highlight LPS phosphate as a critical factor in S. maltophilia's response to gentamicin across different temperatures.

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