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Nucleotide sequence and characterization of a carbenicillin-hydrolyzing penicillinase gene from Proteus mirabilis

Y Sakurai1, K Tsukamoto, T Sawai

  • 1Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Japan.

Journal of Bacteriology
|November 1, 1991
PubMed

Insights

Researchers cloned the carbenicillinase gene from Proteus mirabilis, identifying a novel class A beta-lactamase. This enzyme may not be specific to P. mirabilis, indicating broader implications for antibiotic resistance research.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Beta-lactamase enzymes confer antibiotic resistance.
  • Carbenicillinase, a type of beta-lactamase, is crucial in understanding resistance mechanisms.
  • Proteus mirabilis is a known bacterium carrying resistance genes.

Purpose of the Study:

  • To clone and characterize the structural gene for carbenicillinase from Proteus mirabilis GN79.
  • To determine the class and unique features of the resulting beta-lactamase enzyme.
  • To investigate the species specificity of the identified carbenicillinase.

Main Methods:

  • Cloning of the structural gene from chromosomal DNA.
  • Amino acid sequence alignment with known beta-lactamases.
  • DNA hybridization techniques using a DNA fragment probe.

Main Results:

  • The structural gene codes for a 270-amino acid protein.
  • The enzyme is identified as a novel class A beta-lactamase with a unique RTG conserved triad.
  • DNA hybridization confirmed the carbenicillinase gene is not species-specific to P. mirabilis isolates.

Conclusions:

  • A novel class A beta-lactamase with unique features has been identified.
  • The carbenicillinase identified in this study is likely not specific to Proteus mirabilis.
  • Findings contribute to understanding the evolution and spread of antibiotic resistance genes.

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