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Antimicrobial Agents and Chemotherapy, February 2008, p. 626-630, Vol. 52, No. 2
0066-4804/08/$08.00+0 doi:10.1128/AAC.01126-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Service de Microbiologie and EA 2128 Relations hôte et microorganismes des épithéliums, Hôpital Côte de Nacre, Université de Caen Basse-Normandie, 14033 Caen Cedex, France,1 Department of Microbiology, Medical School, University of Thessalia, Larissa 41112, Greece,2 Université de Lyon 1, Laboratoire de Biométrie et Biologie Evolutive (UMR5558), CNRS, Faculté de Médecine Lyon sud, 69921 Oullins Cedex, France,3 Laboratoire de Microbiologie de l'Environnement, USC INRA EA956, IRBA, Université de Caen Basse-Normandie, France4
Received 25 August 2007/ Returned for modification 23 October 2007/ Accepted 3 December 2007
Streptococcus uberis UCN 42, isolated from a case of bovine mastitis, was intermediately resistant to lincomycin (MIC = 2 µg/ml) while remaining susceptible to clindamycin (MIC = 0.06 µg/ml) and erythromycin. A 1.1-kb SacI fragment was cloned from S. uberis UCN 42 total DNA on plasmid pUC 18 and introduced into Escherichia coli AG100A, where it conferred resistance to both clindamycin and lincomycin. The sequence analysis of the fragment showed the presence of a new gene, named lnu(D), that encoded a 164-amino-acid protein with 53% identity with Lnu(C) previously reported to occur in Streptococcus agalactiae. Crude lysates of E. coli AG100A containing the cloned lnu(D) gene inactivated lincomycin and clindamycin in the presence of ATP and MgCl2. Mass spectrometry experiments demonstrated that the lnu(D) enzyme catalyzed adenylylation of clindamycin. A domain conserved in deduced sequences of lincosamide O-nucleotidyltransferases Lnu(A), Lnu(C), LinAN2, and Lin(D) and in the aminoglycoside nucleotidyltransferase ANT(2'') was identified.
Published ahead of print on 17 December 2007.
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