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A beta-lactamase belonging to group 2e from oral clinical isolates of Prevotella intermedia

G Valle1, L M Quirós, M T Andrés

  • 1Laboratory of Oral Microbiology, Faculty of Medicine, University of Oviedo, 3306 Oviedo, Spain.

FEMS Microbiology Letters
|June 12, 2001
PubMed

Insights

A novel beta-lactamase enzyme from Prevotella intermedia, identified as a 2e-cephalosporinase, effectively hydrolyzes cefuroxime and cephalothin. This enzyme is potently inhibited by clavulanic acid, tazobactam, and sulbactam.

Area of Science:

  • Microbiology
  • Enzymology
  • Pharmacology

Background:

  • Prevotella intermedia is a common bacterium found in oral infections.
  • Beta-lactamase enzymes contribute to antibiotic resistance in bacteria.
  • Understanding novel beta-lactamases is crucial for developing effective treatments.

Purpose of the Study:

  • To characterize a beta-lactamase enzyme from clinical isolates of Prevotella intermedia.
  • To determine the substrate specificity and inhibition profile of the identified enzyme.

Main Methods:

  • Enzyme purification and characterization.
  • Hydrolysis rate determination using cephalosporins.
  • Inhibition assays with various beta-lactamase inhibitors.

Main Results:

  • A beta-lactamase, classified as a 2e-cephalosporinase, was identified in Prevotella intermedia.
  • The enzyme showed significant hydrolysis rates for cefuroxime and cephalothin.
  • Clavulanic acid, tazobactam, and sulbactam demonstrated potent inhibition (IC50 values: 0.72, 0.21, and 0.07 microM, respectively).
  • The enzyme was not inhibited by cloxacillin, EDTA, NaCl, or p-CMB.
  • Isoelectric point (pI) was 4.7 and pH optimum was 5.4.

Conclusions:

  • Prevotella intermedia possesses a 2e-cephalosporinase with activity against key cephalosporins.
  • The enzyme's susceptibility to common beta-lactamase inhibitors suggests potential therapeutic strategies.
  • Further research into this enzyme could aid in combating Prevotella-associated infections.

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