A plasmid-mediated CMY-2 β-lactamase from an Algerian clinical isolate of Salmonella senftenberg

• Published in: FEMS microbiology letters 1997-07, Vol.152 (2), p.255-260
• Main Authors: Koeck, Jean-Louis, Arlet, Guillaume, Philippon, Alain, Basmaciogullari, Stéphane, Thien, Hoang Vu, Buisson, Yves, Cavallo, Jean-Didier
• Format: Article
• Language: English
• Subjects: Algeria; Amino acid sequence; Amino acids; ampC gene; Anti-Bacterial Agents - pharmacology; Antibiotics; beta-Lactam Resistance - genetics; beta-Lactamases - genetics; beta-Lactams - pharmacology; Biochemical analysis; Cefoxitin; Child; Conjugation; Drug Resistance, Multiple - genetics; E coli; Escherichia coli; Feces - microbiology; Humans; Microbial Sensitivity Tests; Microbiology; Molecular Sequence Data; Plasmids - genetics; Plasmid‐mediated β‐lactamase; Salmonella; Salmonella - drug effects; Salmonella - enzymology; Salmonella - genetics; Salmonella - isolation & purification; Salmonella senftenberg; Substrate inhibition; β-Lactam antibiotics
• ISSN: 0378-1097; 1574-6968
• DOI: 10.1111/j.1574-6968.1997.tb10436.x

Abstract Multiresistance to antibiotics including β-lactams, e.g. cefoxitin, was transferred by conjugation to Escherichia coli strain C1a from a clinical isolate of Salmonella senftenberg recovered from stools of an Algerian child. The susceptibility pattern to β-lactams was similar to the profile mediated by an AmpC-type β-lactamase. By biochemical analysis, typical AmpC-type enzyme substrate and inhibition profiles were obtained. Finally, an amp C plasmid-encoded β-lactamase gene was cloned and sequenced. Its deduced amino acid sequence confirmed its identity as a class C β-lactamase. It showed 99.5% sequence identity with the plasmid-mediated β-lactamase CMY-2. The differences in the amino acid sequences of the two enzymes were located in the signal peptide.