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Aminoglycoside-modifying enzymes in clinical isolates harboring extended-spectrum beta-lactamases

A Fernandez-Rodriguez1, R Canton, J C Perez-Diaz

  • 1Servicio de Microbiología, Hospital Clínico de San Carlos, Madrid, Spain.

Antimicrobial Agents and Chemotherapy
|November 1, 1992
PubMed

Insights

Extended-spectrum beta-lactamases (ESBLs) are common in Spanish clinical isolates. Most ESBL-producing bacteria were resistant to gentamicin, with specific aminoglycoside-modifying enzymes frequently identified.

Area of Science:

  • Microbiology
  • Antimicrobial Resistance
  • Enzyme activity

Background:

  • Extended-spectrum beta-lactamases (ESBLs) are a significant cause of bacterial resistance.
  • Aminoglycoside-modifying enzymes (AMEs) contribute to aminoglycoside resistance.
  • Understanding enzyme prevalence is crucial for effective treatment strategies.

Purpose of the Study:

  • To identify and characterize aminoglycoside-modifying enzymes in clinical isolates harboring ESBLs.
  • To determine the prevalence of gentamicin resistance in these isolates.
  • To investigate the co-transfer of AMEs with specific ESBL types.

Main Methods:

  • Analysis of 120 clinical isolates from Spain.
  • Detection of extended-spectrum beta-lactamases (ESBLs).
  • Identification of aminoglycoside-modifying enzymes (AMEs) using molecular methods.

Main Results:

  • 84% of the clinical isolates exhibited gentamicin resistance.
  • The most frequent AMEs identified were AAC(3)V, APH(3"), and APH(3")I.
  • These enzymes were frequently associated and co-transferred with SHV-2 or TEM-type beta-lactamases.

Conclusions:

  • Gentamicin resistance is highly prevalent in ESBL-producing clinical isolates in Spain.
  • Specific AMEs, including AAC(3)V, APH(3"), and APH(3")I, are key contributors to this resistance.
  • The co-transfer of these AMEs with ESBLs highlights the challenge of managing multidrug-resistant bacteria.

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