Interaction of FCE 22101 with penicillin-binding proteins of Staphylococcus aureus.
AUTOR(ES)
Tonin, E A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=171435Documentos Relacionados
- Possible physiological functions of penicillin-binding proteins in Staphylococcus aureus.
- Altered penicillin-binding proteins in methicillin-resistant strains of Staphylococcus aureus.
- Regulation of penicillin-binding protein activity: description of a methicillin-inducible penicillin-binding protein in Staphylococcus aureus.
- Increased production of penicillin-binding protein 2, increased detection of other penicillin-binding proteins, and decreased coagulase activity associated with glycopeptide resistance in Staphylococcus aureus.
- Low-affinity penicillin-binding protein associated with beta-lactam resistance in Staphylococcus aureus.