2″-O-Phosphorylation of Gentamicin Components by a Staphylococcus aureus Strain Carrying a Plasmid
AUTOR(ES)
Goffic, F. Le
RESUMO
A wild-type strain of Staphylococcus aureus that inactivates the 4,6-glycosidically linked deoxystreptamine aminoglycoside antibiotics by a plasmid-mediated process was found to harbor two enzymes: an acetyltransferase of the AAC(6′) type and a new phosphotranferase specific to the gentamicin components. The target of this last enzyme is the 2″-hydroxyl function of these antibiotics, since one inactivated compound is 2″-(O)-phosphorylsisomicin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=352148Documentos Relacionados
- New Exfoliative Toxin Produced by a Plasmid-Carrying Strain of Staphylococcus hyicus
- Plasmid-Mediated Resistance to Gentamicin in Staphylococcus aureus
- Gentamicin uptake in Staphylococcus aureus possessing plasmid-encoded, aminoglycoside-modifying enzymes.
- Aminoglycoside Modification by Gentamicin-Resistant Isolates of Staphylococcus aureus
- An outbreak of infection caused by a gentamicin-resistant Staphylococcus aureus.
