Unusual tazobactam-sensitive AmpC β-lactamase from two Escherichia coli isolates

Gioia S. Babini; Franck Danel; Susan D. Munro; Patricia A. Micklesen; David M. Livermore

doi:10.1093/jac/41.1.115

Unusual tazobactam-sensitive AmpC β-lactamase from two Escherichia coli isolates

Gioia S. Babini, Franck Danel, Susan D. Munro, Patricia A. Micklesen, David M. Livermore^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

Two Escherichia coli isolates were studied. MIC patterns and hydrolysis assays suggested that they hyperproduced AmpC β-lactamase, but synergy between ceftazidime and tazobactam was greater than between ceftazidime and Ro 48-1256, whereas the converse pattern is typical of AmpC hyperproducers. Studies with purified β-lactamase from one of the isolates confirmed that tazobactam was a 100-fold stronger inhibitor than for the classical E. coli AmpC enzyme. Moreover, in contrast to typical AmpC types, the new enzyme had greater affinity for cephaloridine than for benzylpenicillin.

Original language	English
Pages (from-to)	115-118
Number of pages	4
Journal	Journal of Antimicrobial Chemotherapy
Volume	41
Issue number	1
DOIs	https://doi.org/10.1093/jac/41.1.115
Publication status	Published - Jan 1998

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title = "Unusual tazobactam-sensitive AmpC β-lactamase from two Escherichia coli isolates",

abstract = "Two Escherichia coli isolates were studied. MIC patterns and hydrolysis assays suggested that they hyperproduced AmpC β-lactamase, but synergy between ceftazidime and tazobactam was greater than between ceftazidime and Ro 48-1256, whereas the converse pattern is typical of AmpC hyperproducers. Studies with purified β-lactamase from one of the isolates confirmed that tazobactam was a 100-fold stronger inhibitor than for the classical E. coli AmpC enzyme. Moreover, in contrast to typical AmpC types, the new enzyme had greater affinity for cephaloridine than for benzylpenicillin.",

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AU - Babini, Gioia S.

AU - Danel, Franck

AU - Munro, Susan D.

AU - Micklesen, Patricia A.

AU - Livermore, David M.

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N2 - Two Escherichia coli isolates were studied. MIC patterns and hydrolysis assays suggested that they hyperproduced AmpC β-lactamase, but synergy between ceftazidime and tazobactam was greater than between ceftazidime and Ro 48-1256, whereas the converse pattern is typical of AmpC hyperproducers. Studies with purified β-lactamase from one of the isolates confirmed that tazobactam was a 100-fold stronger inhibitor than for the classical E. coli AmpC enzyme. Moreover, in contrast to typical AmpC types, the new enzyme had greater affinity for cephaloridine than for benzylpenicillin.

AB - Two Escherichia coli isolates were studied. MIC patterns and hydrolysis assays suggested that they hyperproduced AmpC β-lactamase, but synergy between ceftazidime and tazobactam was greater than between ceftazidime and Ro 48-1256, whereas the converse pattern is typical of AmpC hyperproducers. Studies with purified β-lactamase from one of the isolates confirmed that tazobactam was a 100-fold stronger inhibitor than for the classical E. coli AmpC enzyme. Moreover, in contrast to typical AmpC types, the new enzyme had greater affinity for cephaloridine than for benzylpenicillin.

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Unusual tazobactam-sensitive AmpC β-lactamase from two Escherichia coli isolates

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