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Beta-lactamases from Yersinia enterocolitica.

G Cornelis, E P Abraham

    Journal of General Microbiology
    |April 1, 1975
    PubMed
    Summary
    This summary is machine-generated.

    Yersinia enterocolitica produces two beta-lactamases, A and B, with distinct activities and properties. Beta-lactamase B production is selectively increased by 6-aminopenicillanic acid, suggesting a role in ampicillin resistance.

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    Area of Science:

    • Microbiology
    • Enzymology
    • Bacterial Genetics

    Background:

    • Beta-lactamase enzymes confer resistance to beta-lactam antibiotics.
    • Yersinia enterocolitica is an opportunistic pathogen that can acquire antibiotic resistance mechanisms.

    Purpose of the Study:

    • To characterize the beta-lactamase enzymes produced by Yersinia enterocolitica.
    • To investigate the regulation of beta-lactamase production in response to specific compounds.

    Main Methods:

    • Enzyme purification and characterization (hydrolysis profiles, inhibition studies, molecular weight determination).
    • Cultivation of Yersinia enterocolitica strains with and without 6-aminopenicillanic acid.
    • Enzyme activity assays on cell extracts.

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    Main Results:

    • Two distinct beta-lactamases (A and B) were identified in Yersinia enterocolitica strain w222, with differing substrate specificities and sensitivities to inhibitors.
    • Beta-lactamase A (approx. 20 kDa) hydrolyzed penicillins and cephalosporins, while Beta-lactamase B (approx. 34 kDa) showed strong cephalosporinase activity.
    • Beta-lactamase B production was selectively increased (2-4 fold) by 6-aminopenicillanic acid.
    • Similar beta-lactamases were found in other Y. enterocolitica strains, with one ampicillin-sensitive strain (H66) showing an 8-10 fold increase in beta-lactamase B production upon 6-aminopenicillanic acid addition.

    Conclusions:

    • Yersinia enterocolitica possesses multiple beta-lactamase enzymes contributing to antibiotic resistance.
    • The induction of beta-lactamase B by 6-aminopenicillanic acid highlights a regulatory mechanism potentially involved in resistance.
    • Characterization of these enzymes is crucial for understanding and combating antibiotic resistance in Yersinia species.