Characterization of clinical isolates of beta-lactamase-negative, highly ampicillin-resistant Enterococcus faecalis.
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.
Cercenado
E
E
Servicio de Microbiología, Hospital General Universitario Gregorio Marañón, Madrid, Spain.
Vicente
M F
MF
Díaz
M D
MD
Sánchez-Carrillo
C
C
Sánchez-Rubiales
M
M
D000668:Ampicillin Resistance / Q000502:physiology*; D001426:Bacterial Proteins; D002352:Carrier Proteins / Q000378:metabolism; D013293:Enterococcus faecalis / Q000187:drug effects* / Q000201:enzymology*; D016908:Gram-Positive Bacterial Infections / Q000382:microbiology*; D006602:Hexosyltransferases; D006801:Humans; D002267:Muramoylpentapeptide Carboxypeptidase / Q000378:metabolism; D046915:Penicillin-Binding Proteins; D010406:Penicillins / Q000378:metabolism; D010458:Peptidyl Transferases; D001618:beta-Lactamases / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D046915:Penicillin-Binding Proteins; D010406:Penicillins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases