Characterization of clinical isolates of beta-lactamase-negative, highly ampicillin-resistant Enterococcus faecalis.
AUTOR(ES)
Cercenado, E
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=163546Documentos Relacionados
- Simple screening method for beta-lactamase-positive and -negative ampicillin-resistant Haemophilus influenzae isolates.
- Beta-Lactamase Activity in Ampicillin-Resistant Haemophilus influenzae
- Mechanism of resistance of an ampicillin-resistant, beta-lactamase-negative clinical isolate of Haemophilus influenzae type b to beta-lactam antibiotics.
- Molecular Characterization of Ampicillin-Resistant Enterococcus faecium Isolates from Hospitalized Patients in Norway
- Molecular epidemiology of ampicillin-resistant clinical isolates of Salmonella enteritidis.