Interactions of ceftibuten with extended-spectrum beta-lactamases: a bacteriological and enzymatic analysis.
The authors analysed the antibacterial activity of ceftibuten, cefotaxime, ceftazidime and aztreonam against Klebsiella pneumoniae strains, including those which produced novel extended-spectrum beta-lactamases. These molecules were also tested for their susceptibility to cell-free extracts of the corresponding beta-lactamases. Both approaches showed that ceftibuten was not hydrolysed by the CTX-1/TEM-3, SHV-2 and SHV-3 beta-lactamases, while cefotaxime, ceftazidime and aztreonam were hydrolysed. Nevertheless all compounds were substrates for the SHV-4 and SHV-5 beta-lactamases, and the organisms which produced these beta-lactamases showed increased MICs.
Thabaut
A
A
Biology Laboratory, Hospital Bégin, Saint-Mandé.
Meyran
M
M
Sofer
L
L
Morand
A
A
Labia
R
R
D000077722:Ceftibuten; D018550:Cephalosporin Resistance; D002511:Cephalosporins / Q000737:chemistry / Q000494:pharmacology*; D007711:Klebsiella pneumoniae / Q000187:drug effects* / Q000201:enzymology*; D008826:Microbial Sensitivity Tests; D001618:beta-Lactamases / Q000302:isolation & purification / Q000378:metabolism*
D002511:Cephalosporins; D001618:beta-Lactamases; D000077722:Ceftibuten