Publication | Open Access
Characterization of clinical isolates of beta-lactamase-negative, highly ampicillin-resistant Enterococcus faecalis
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Citations
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References
1996
Year
Different PbpsAntimicrobial Resistance GeneAntimicrobial SusceptibilityHealth SciencesAntibioticsAmpicillin-resistant Enterococcus FaecalisMedicineKlebsiella PneumoniaePathologyPbps 1Six PbpsMicrobiologyInfection ControlAntibiotic ResistanceBacterial ResistanceClinical MicrobiologyAntimicrobial ResistanceDrug Resistance
We analyzed the penicillin-binding protein (PBP) profiles of two clinical isolates of Enterococcus faecalis for which ampicillin MICs were 32 and 64 micrograms/ml. Six PBPs were detected in both isolates, demonstrating an apparently increased amount of PBP 5 and decreased penicillin binding of PBPs 1 and 6. These results suggest that ampicillin resistance in the clinical isolates of E. faecalis described could be associated with alterations in different PBPs.
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