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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.

Identification of the Novel Narrow-Spectrum β-Lactamase SCO-1 in Acinetobacter spp. from Argentina