Interaction of FCE 22101 with penicillin-binding proteins of Staphylococcus aureus.
FCE 22101 is a new penem characterized by a broad spectrum of activity which includes activity against methicillin-resistant strains of Staphylococcus aureus. The interaction of FCE 22101 with penicillin-binding protein 2a of a methicillin-resistant S. aureus strain has been investigated in the present study. In competition experiments, the penem showed a very low affinity for this protein, and a concentration more than 4 times the MIC was required for penicillin-binding protein 2a saturation. When the classical competitive procedure was modified by increasing the time of incubation of either membranes or growing cells with FCE 22101, the antibiotic showed a much higher affinity for penicillin-binding protein 2a and saturated the protein at a concentration close to the MIC, with slow kinetics.
Tonin
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EA
Institute of Microbiology, University of Padova, Italy.
Fontana
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R
D000900:Anti-Bacterial Agents / Q000378:metabolism*; D001426:Bacterial Proteins; D015780:Carbapenems; D002352:Carrier Proteins / Q000378:metabolism*; D006602:Hexosyltransferases; D007769:Lactams; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism*; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D013211:Staphylococcus aureus
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D015780:Carbapenems; D002352:Carrier Proteins; D007769:Lactams; D046915:Penicillin-Binding Proteins; C040033:ritipenem; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase