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The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
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The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions

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Plazomicin Is Active Against Metallo-β-Lactamase-Producing Enterobacteriaceae

Alisa W Serio1, Tiffany Keepers1, Kevin M Krause1

  • 1Department of Clinical Microbiology, Achaogen, Inc., South San Francisco, California.

Open Forum Infectious Diseases
|April 11, 2019
PubMed

Insights

Plazomicin, an aminoglycoside antibiotic, treats complicated urinary tract infections. It overcomes common resistance but not target modification by 16S ribosomal RNA methyltransferases (16S-RMTase).

Area of Science:

  • Pharmacology
  • Infectious Diseases
  • Microbiology

Background:

  • Plazomicin is an FDA-approved aminoglycoside for complicated urinary tract infections (cUTIs).
  • It was designed to combat aminoglycoside-modifying enzyme (AME) resistance.
  • However, plazomicin is ineffective against 16S ribosomal RNA methyltransferases (16S-RMTase) mediated resistance.

Purpose of the Study:

  • To evaluate plazomicin's activity against Enterobacteriaceae, particularly those with metallo-β-lactamase (MBL) resistance.
  • To understand plazomicin's efficacy in the context of prevalent and emerging antibiotic resistance mechanisms.

Main Methods:

  • In vitro susceptibility testing of plazomicin against a panel of Enterobacteriaceae isolates.
  • Analysis of resistance mechanisms, including AMEs and 16S-RMTases.
  • Assessment of plazomicin activity against MBL-producing strains.

Main Results:

  • Plazomicin demonstrated activity against Enterobacteriaceae producing common AMEs.
  • Activity was retained against strains expressing metallo-β-lactamases (MBLs) in the absence of 16S-RMTase.
  • Resistance to plazomicin was observed in strains harboring 16S-RMTases.

Conclusions:

  • Plazomicin is a valuable therapeutic option for cUTIs caused by susceptible Enterobacteriaceae, including MBL producers lacking 16S-RMTase.
  • The emergence of 16S-RMTase poses a significant resistance challenge to plazomicin.
  • Understanding resistance mechanisms is crucial for optimizing plazomicin use in clinical settings.
Keywords:
aminoglycosidemetallo-β-lactamaseplazomicin

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