Oxacillin-hydrolyzing beta-lactamase involved in resistance to imipenem in Acinetobacter baumannii.

Abstract:

:Acinetobacter baumannii strain A148, a clinical isolate resistant to imipenem (MIC = 32 mg l-1), synthesized two beta-lactamases with pIs 6.3 and > 9.2. The pI 6.3 enzyme hydrolyzed the penicillins, including isoxazoylpenicillins, first-, second- and, to a lesser extent, third-generation cephalosporins. It was inhibited by chloride ions and by the penem beta-lactamase inhibitor BRL 42715. Clavulanate was a weak inhibitor and EDTA did not affect the beta-lactamase activity. This enzyme also hydrolyzed imipenem with a catalytic efficiency (Kcat/Km) of 1500 mM-1 s-1. Moreover, this purified beta-lactamase produced a positive microbiological clover-leaf test with imipenem. Therefore, the pI 6.3 beta-lactamase was considered to be involved in the imipenem resistance of A. baumannii strain A148.

journal_name

FEMS Microbiol Lett

authors

Hornstein M,Sautjeau-Rostoker C,Péduzzi J,Vessières A,Hong LT,Barthélémy M,Scavizzi M,Labia R

doi

10.1111/j.1574-6968.1997.tb12593.x

subject

Has Abstract

pub_date

1997-08-15 00:00:00

pages

333-9

issue

2

eissn

0378-1097

issn

1574-6968

pii

S037810979700270X

journal_volume

153

pub_type

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