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Characterization of a new plasmid-mediated extended-spectrum beta-lactamase from Serratia marcescens

C Kunugita1, F Higashitani, A Hyodo

  • 1Anticancer and Antimicrobial Research Lab, Taiho Pharmaceutical Co, Ltd, Tokushima, Japan.

Insights

A novel extended-spectrum beta-lactamase, CKH-1, was identified in Serratia marcescens from complicated urinary tract infections. This enzyme confers resistance to various beta-lactams, indicating a new threat in antimicrobial resistance.

Area of Science:

  • Microbiology
  • Biochemistry

Background:

  • Complicated urinary tract infections (cUTIs) pose a significant therapeutic challenge.
  • The emergence of antimicrobial resistance, particularly beta-lactamase production in Gram-negative bacteria, is a growing global health concern.
  • Serratia marcescens is an opportunistic pathogen frequently associated with healthcare-associated infections.

Purpose of the Study:

  • To characterize a newly identified extended-spectrum beta-lactamase (ESBL) produced by a clinical isolate of Serratia marcescens.
  • To investigate the enzymatic properties and resistance profile conferred by this novel beta-lactamase.
  • To determine the genetic basis and transferability of the beta-lactamase genes.

Main Methods:

  • Isolation and identification of Serratia marcescens from patient urine samples.
  • Detection and characterization of beta-lactamase activity using biochemical assays.
  • Gene conjugation experiments to transfer beta-lactamase encoding genes to Escherichia coli.
  • Purification and kinetic analysis of the novel beta-lactamase (CKH-1).
  • Determination of minimum inhibitory concentrations (MICs) for various beta-lactam antibiotics.

Main Results:

  • A clinical isolate of Serratia marcescens (strain 42039) produced three beta-lactamases: TEM-1, a cephalosporinase, and a novel ESBL, CKH-1.
  • Genes encoding TEM-1 and CKH-1 were successfully transferred to Escherichia coli K-12 via conjugation.
  • The transconjugant strains exhibited high-level resistance to ampicillin, piperacillin, and cephalothin, with reduced susceptibility to ceftazidime, cefotaxime, and ceftriaxone.
  • Purified CKH-1 enzyme (30 kDa, pI 8.2) demonstrated broad-spectrum activity, hydrolyzing cephalothin and oxyiminocephalosporins.
  • CKH-1 showed potent inhibition by tazobactam and BRL-42715, classifying it as a Class A beta-lactamase.

Conclusions:

  • CKH-1 represents the first reported plasmid-mediated oxyiminocephalosporin-hydrolyzing ESBL from clinical Serratia marcescens isolates.
  • The discovery of CKH-1 highlights the evolving landscape of beta-lactamase resistance in S. marcescens.
  • This finding underscores the need for continuous surveillance and development of strategies to combat emerging antimicrobial resistance.

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