• Medientyp: E-Artikel
  • Titel: A New Resistance Gene, linB , Conferring Resistance to Lincosamides by Nucleotidylation in Enterococcus faecium HM1025
  • Beteiligte: Bozdogan, Bülent; Berrezouga, Latifa; Kuo, Ming-Shang; Yurek, David A.; Farley, Kathleen A.; Stockman, Brian J.; Leclercq, Roland
  • Erschienen: American Society for Microbiology, 1999
  • Erschienen in: Antimicrobial Agents and Chemotherapy
  • Sprache: Englisch
  • DOI: 10.1128/aac.43.4.925
  • ISSN: 0066-4804; 1098-6596
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  • Beschreibung: <jats:title>ABSTRACT</jats:title> <jats:p> Resistance to lincomycin and clindamycin in the clinical isolate <jats:italic>Enterococcus faecium</jats:italic> HM1025 is due to a ribosomal methylase encoded by an <jats:italic>ermAM</jats:italic> -like gene and the plasmid-mediated inactivation of these antibiotics. We have cloned and determined the nucleotide sequence of the gene responsible for the inactivation of lincosamides, <jats:italic>linB</jats:italic> . This gene encodes a 267-amino-acid lincosamide nucleotidyltransferase. The enzyme catalyzes 3-(5′-adenylation) (the adenylation of the hydroxyl group in position 3 of the molecules) of lincomycin and clindamycin. Expression of <jats:italic>linB</jats:italic> was observed in both <jats:italic>Escherichia coli</jats:italic> and <jats:italic>Staphylococcus aureus</jats:italic> . The deduced amino acid sequence of the enzyme did not display any significant homology with staphylococcal nucleotidyltransferases encoded by <jats:italic>linA</jats:italic> and <jats:italic>linA</jats:italic> ′ genes. Sequences homologous to <jats:italic>linB</jats:italic> were found in 14 other clinical isolates of <jats:italic>E. faecium</jats:italic> , indicating the spread of the resistance trait in this species. </jats:p>
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