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Antimicrobial Agents and Chemotherapy, April 1999, p. 925-929, Vol. 43, No. 4
Service de Bactériologie-Virologie,
Received 3 August 1998/Returned for modification 15 September
1998/Accepted 6 January 1999
Resistance to lincomycin and clindamycin in the clinical isolate
Enterococcus faecium HM1025 is due to a ribosomal methylase encoded by an ermAM-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, linB. 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
linB was observed in both Escherichia coli and
Staphylococcus aureus. The deduced amino acid sequence of
the enzyme did not display any significant homology with staphylococcal nucleotidyltransferases encoded by linA and
linA' genes. Sequences homologous to linB were
found in 14 other clinical isolates of E. faecium,
indicating the spread of the resistance trait in this species.
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
A New Resistance Gene, linB, Conferring
Resistance to Lincosamides by Nucleotidylation in
Enterococcus faecium HM1025
Université Paris XII,
*
Corresponding author. Mailing address: CHU de Caen,
Service de Microbiologie, Avenue Côte de Nacre, 14033 Caen cedex,
France. Phone: (33) 2 31 06 45 72. Fax: (33) 2 31 06 45 73. E-mail:
leclercq-r{at}chu-caen.fr.
Antimicrobial Agents and Chemotherapy, April 1999, p. 925-929, Vol. 43, No. 4
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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