1. Identification of the novel narrow-spectrum beta-lactamase SCO-1 in Acinetobacter spp. from Argentina.
- Author
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Poirel L, Corvec S, Rapoport M, Mugnier P, Petroni A, Pasteran F, Faccone D, Galas M, Drugeon H, Cattoir V, and Nordmann P
- Subjects
- Acinetobacter classification, Acinetobacter genetics, Acinetobacter Infections microbiology, Amino Acid Sequence, Argentina, Clavulanic Acid metabolism, Clavulanic Acid pharmacology, Cloning, Molecular, Humans, Microbial Sensitivity Tests, Molecular Sequence Data, Sequence Analysis, DNA, Acinetobacter drug effects, Acinetobacter enzymology, Anti-Bacterial Agents pharmacology, beta-Lactam Resistance, beta-Lactamases chemistry, beta-Lactamases genetics, beta-Lactamases isolation & purification, beta-Lactamases metabolism, beta-Lactams pharmacology
- Abstract
By studying the beta-lactamase content of several Acinetobacter spp. isolates from Argentina, producing the expanded-spectrum beta-lactamases (ESBL) VEB-1a or PER-2, a novel Ambler class A beta-lactamase gene was identified. It encoded the narrow-spectrum beta-lactamase SCO-1, whose activity was inhibited by clavulanic acid. SCO-1 hydrolyzes penicillins at a high level and cephalosporins and carbapenems at a very low level. beta-Lactamase SCO-1 was identified from unrelated VEB-1a-positive or PER-2-positive Acinetobacter spp. isolates recovered from three hospitals. The bla(SCO-1) gene was apparently located on a plasmid of ca. 150 kb from all cases but was not associated with any ESBL-encoding gene. The G+C content of the bla(SCO) gene was 52%, a value that does not correspond to that of the A. baumannii genome (39%). beta-Lactamase SCO-1 shares 47% amino acid identity with CARB-5 and ca. 40% with the enzymes TEM, SHV, and CTX-M. A gene encoding a putative resolvase was identified downstream of the bla(SCO-1) gene, but its precise way of acquisition remains to be determined.
- Published
- 2007
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