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Related Experiment Videos

OXA-type beta-lactamases.

T Naas1, P Nordmann

  • 1Service de Bactériologie-Virologie, Hôpital de Bicêtre, 94274 Le Kremlin-Bicêtre, Assistance Publique-Hôpitaux de Paris, Faculté de Médecine Paris-Sud, Université Paris XI, Paris, France. thierry.naas@kb.u-psud.fr

Current Pharmaceutical Design
|December 14, 1999
PubMed
Summary

OXA-type enzymes confer penicillin resistance in bacteria like E. coli and P. aeruginosa. Sodium chloride strongly inhibits these oxacillin-hydrolysing beta-lactamases, unlike clavulanic acid.

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Area of Science:

  • Microbiology
  • Enzymology
  • Structural Biology

Background:

  • OXA-type enzymes, or oxacillin-hydrolysing beta-lactamases, are prevalent in Enterobacteriaceae and Pseudomonas aeruginosa.
  • These enzymes confer resistance to various penicillins and exhibit potent hydrolytic activity against cloxacillin, oxacillin, and methicillin.
  • While clavulanic acid offers weak inhibition, sodium chloride demonstrates strong inhibitory effects on OXA-type enzyme activity.

Purpose of the Study:

  • To review the characteristics and known diversity of OXA-type beta-lactamases.
  • To highlight the structural and functional properties of these Ambler class D enzymes.
  • To discuss the implications of their genetic location and potential for resistance spread.

Main Methods:

  • Literature review of characterized OXA-type enzymes.

Related Experiment Videos

  • Analysis of sequence and biochemical data for Ambler class D beta-lactamases.
  • Comparison of amino-acid identities among different OXA enzyme subclasses.

    • Main Results:

    • Twenty-four Ambler class D enzymes (OXA-1 to OXA-22, AmpS, LCR-1) have been characterized, but none have available 3D structures.
    • Most OXA enzymes show limited amino-acid identity (20-30%), though some exhibit higher relatedness (e.g., OXA-1 and OXA-4).
    • Mutations in OXA-2 or OXA-10 derivatives have led to expanded resistance spectra, including cephalosporins and imipenem.

    Conclusions:

    • OXA-type beta-lactamases are diverse Ambler class D enzymes with varying degrees of sequence identity.
    • Despite typically restricted resistance phenotypes, mutations can extend their spectrum, posing a significant clinical challenge.
    • Plasmid and integron locations facilitate the widespread dissemination of these important resistance determinants.