Affiliation:
1. Unité des Agents Antibactériens, Institut Pasteur, 75724 Paris Cedex 15, France1;
2. Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom2; and
3. MRL Pharmaceutical Services, Herndon, Virginia 201713
Abstract
ABSTRACT
Enterococcus faecalis
BM4405 was resistant to low levels of vancomycin (MIC, 16 μg/ml) and was susceptible to teicoplanin (MIC, 0.5 μg/ml). No PCR product was obtained when the total DNA of this clinical isolate was used as a template with primers specific for glycopeptide resistance genes
vanA
,
vanB
,
vanC
, and
vanD
. However, a 604-bp PCR fragment was obtained when V1 and V2 degenerate primers were used and total DNA was digested with
Hin
dIII as a template. The product was cloned and sequenced. The deduced amino acid sequence had greater identity (55%) with VanC than with VanA (45%), VanB (43%), or VanD (44%). This was consistent with the fact that BM4405 synthesized peptidoglycan precursors that terminated in
d
-serine residues. After induction with vancomycin, weak
d
,
d
-dipeptidase and penicillin-insensitive
d
,
d
-carboxypeptidase activities were detected in cytoplasmic extracts of BM4405, whereas a serine racemase activity was found in the membrane preparation. This new type of acquired glycopeptide resistance was named VanE.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
204 articles.
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