Two novel transferable extended-spectrum beta-lactamases from Klebsiella pneumoniae in Tunisia.
Two novel beta-lactamases conferring multiresistance to antibiotics including oxyimino beta-lactams have been identified in two nosocomial K. pneumoniae strains isolated in Tunis in 1986 and 1988. Both enzymes were encoded by ca. 150-kilobase plasmids. Donor and transconjugant strains producing these enzymes exhibited highly similar pattern of resistance (CTX phenotype) to beta-lactams including penicillins and oxyimino beta-lactams e.g. cefotaxime, ceftriaxone, ceftazidime, and aztreonam. High and variable synergy (16 to 1066-fold) was obtained when combined to 0.1 microgram/ml of clavulanate (beta-lactamase inhibitor). The isoelectric points of these two enzymes were 5.4 and 6.4. These beta-lactamases differed from TEM types by hydrolysis for cefotaxime or ceftriaxone but were inhibited by clavulanate and cloxacillin. DNA hybridization studies suggested that that the genes of these enzymes may be derived from genes encoding TEM-type enzymes.
Hôpital Charles Nicolle, Service de Bactériologie-Virologie, Tunis, Tunisie.
S
S
Ben Redjeb
G
G
Fournier
C
C
Mabilat
A
A
Ben Hassen
A
A
Philippon
D004269:DNA, Bacterial / Q000235:genetics; D004352:Drug Resistance, Microbial / Q000235:genetics; D006801:Humans; D007526:Isoelectric Point; D007711:Klebsiella pneumoniae / Q000201:enzymology* / Q000235:genetics / Q000302:isolation & purification; D009693:Nucleic Acid Hybridization; D014416:Tunisia; D001618:beta-Lactamases / Q000235:genetics / Q000378:metabolism*
D004269:DNA, Bacterial; D001618:beta-Lactamases