Characterization of a nosocomial outbreak caused by a multiresistant Acinetobacter baumannii strain with a carbapenem-hydrolyzing enzyme:: High-level carbapenem resistance in A. baumannii is not due solely to the presence of β-lactamases

被引:194
作者
Bou, G
Cerveró, G
Domínguez, MA
Quereda, C
Martínez-Beltrán, J
机构
[1] Hosp Ramon y Cajal, Microbiol Serv, E-28034 Madrid, Spain
[2] CSUB, Bellvitge Hosp, Microbiol Serv, Barcelona, Spain
关键词
D O I
10.1128/JCM.38.9.3299-3305.2000
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
From February to November 1997, 29 inpatients at Ramon y Cajal Hospital, Madrid, Spain, were determined to be either colonized or infected with imipenem- and meropenem-resistant Acinetobacter baumannii (IMRAB) strains (MICs, 128 to 256 mu g/ml). A wide antibiotic multiresistance profile was observed with IMRAB strains. For typing IMRAB isolates, pulsed-field gel electrophoresis was used. For comparative purposes, 30 imipenem- and meropenem-susceptible A. baumannii (IMSAB) strains isolated before, during, and after the outbreak were included in this study. The molecular-typing results showed that the outbreak was caused by a single IMRAB strain (genotype A). By cloning experiments we identified a class D beta-lactamase (OXA-24) encoded in the chromosomal DNA of this IMRAB strain which showed carbapenem hydrolysis. Moreover, the outer membrane profile of the IMRAB strain showed a reduction in the expression of two porins at 22 and 33 kDa when compared with genetically related IMSAB isolates. In addition no efflux mechanisms were identified in the IMRAB strains. In summary, we report here the molecular characterization of a nosocomial outbreak caused by one multiresistant A. baumannii epidemic strain that harbors a carbapenem-hydrolyzing enzyme. Although alterations in the penicillin-binding proteins cannot be ruled out, the reduction in the expression of two porins and the presence of this OXA-derived beta-lactamase are involved in the carbapenem resistance of the epidemic nosocomial IMRAB strain.
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页码:3299 / 3305
页数:7
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