Two novel plasmid-mediated cefotaxime-hydrolyzing β-lactamases (CTX-M-5 and CTX-M-6) from Salmonella typhimurium

Two novel plasmid-mediated β-lactamases (CTX-M-5 and CTX-M-6) produced by Salmonella typhimurium clinical strains were characterized. The enzymes exhibited a p I of 8.4, hydrolyzed oxyimino-β-lactams and were susceptible to mechanism-based β-lactamase inhibitors. The respective bla genes were cloned...

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Veröffentlicht in:	FEMS microbiology letters 1998-08, Vol.165 (2), p.289-293
Hauptverfasser:	Gazouli, Maria, Tzelepi, Eva, Markogiannakis, Antonios, Legakis, Nicholas J, Tzouvelekis, Leonidas S
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Anti-Bacterial Agents - pharmacology Bacteriology Base Sequence beta-Lactamases - chemistry beta-Lactamases - genetics beta-Lactamases - metabolism Biological and medical sciences Cefotaxime Cefotaxime - metabolism Cefotaxime - pharmacology Cephalosporin Resistance - genetics Cephalosporins - metabolism Cephalosporins - pharmacology Fundamental and applied biological sciences. Psychology Genes, Bacterial Genetics Humans Microbial Sensitivity Tests Microbiology Molecular Sequence Data Plasmids - genetics Resistance Salmonella typhimurium Salmonella typhimurium - drug effects Salmonella typhimurium - enzymology Salmonella typhimurium - genetics Sequence Analysis, DNA β-Lactamase
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Zusammenfassung:	Two novel plasmid-mediated β-lactamases (CTX-M-5 and CTX-M-6) produced by Salmonella typhimurium clinical strains were characterized. The enzymes exhibited a p I of 8.4, hydrolyzed oxyimino-β-lactams and were susceptible to mechanism-based β-lactamase inhibitors. The respective bla genes were cloned and sequenced. The deduced amino acid sequences showed a high degree of homology with those of the previously described plasmid class A CTX-M-type enzymes and appeared related to the chromosomal β-lactamases of Klebsiella oxytoca.
ISSN:	0378-1097 1574-6968
DOI:	10.1016/S0378-1097(98)00290-0