Journal of Antimicrobial Chemotherapy (1999) 43, 127-131
© 1999 The British Society for Antimicrobial Chemotherapy
Brief reports |
Biochemical characteristics of a carbapenemase from an Acinetobacter baumannii isolate collected in Buenos Aires, Argentina
a Antibiotic Reference Unit, Central Public Health Laboratory, 61 Colindale Avenue, London NW9 5HT, UK b Catedra de Infectologia y Microbiologia Clinica, Facultad de Post Grado en Ciencias de la Salud, Universidad Catolica Argentina, Adolfo Davila 1500, 1107 Buenos Aires, Argentina
Abstract
Three carbapenem-resistant Acinetobacter baumannii isolates were collected at a hospital in Buenos Aires, Argentina. Isoelectric focusing revealed multiple ß-lactamases, with two of the isolates showing identical profiles. A pI 6.9 carbapenemase with a molecular weight of 30 kDa was purified from one of these two isolates. The enzyme was predominantly a penicillinase, with its highest Vmax for oxacillin but highest VmaxKmfor benzylpenicillin. First-generation cephalosporins and imipenem were weaker substrates than penicillins, and oxyimino-aminothiazolyl cephalosporins were essentially stable. Meropenem-hydrolysing activity was not detected, despite resistance. The carbapenemase was inhibited by clavulanic acid and tazobactam, but not by EDTA. These kinetics place the enzyme into functional group 2; as an oxacillinase it could be placed in sub-group 2d or, as a zinc-independent carbapenemase, in sub-group 2f.
Notes
* Corresponding author. Tel +44-818-200-4400; Fax: +44-181-200-7499; E-mail: dlivermore{at}phls.co.uk
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