Abstract
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.
MeSH terms
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Ampicillin Resistance / physiology*
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Bacterial Proteins*
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Carrier Proteins / metabolism
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Enterococcus faecalis / drug effects*
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Enterococcus faecalis / enzymology*
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Gram-Positive Bacterial Infections / microbiology*
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Hexosyltransferases*
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Humans
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Muramoylpentapeptide Carboxypeptidase / metabolism
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Penicillin-Binding Proteins
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Penicillins / metabolism
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Peptidyl Transferases*
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beta-Lactamases / metabolism*
Substances
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Bacterial Proteins
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Carrier Proteins
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Penicillin-Binding Proteins
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Penicillins
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Peptidyl Transferases
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Hexosyltransferases
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Muramoylpentapeptide Carboxypeptidase
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beta-Lactamases