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

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

Research output: Contribution to journalArticlepeer-review

11 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 languageEnglish
Pages (from-to)115-118
Number of pages4
JournalJournal of Antimicrobial Chemotherapy
Volume41
Issue number1
DOIs
Publication statusPublished - Jan 1998

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