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Journal of Bacteriology, June 1999, p. 3644-3648, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Characterization of the vanD Glycopeptide Resistance Gene Cluster from Enterococcus faecium BM4339

Barbara Casadewall and Patrice Courvalin*

Unité des Agents Antibactériens, Institut Pasteur, 75724 Paris Cedex 15, France

Received 2 March 1999/Accepted 12 April 1999

VanD-type resistance to glycopeptides in Enterococcus faecium BM4339 is due to constitutive synthesis of D-alanyl-D-lactate-terminating peptidoglycan precursors (B. Périchon, P. Reynolds, and P. Courvalin, Antimicrob. Agents Chemother. 41:2016-2018, 1997). The sequence of a 5,780-bp fragment was determined and revealed six open reading frames. The 3' distal part encoded the VanHD dehydrogenase, the VanD ligase, and the VanXD DD-dipeptidase, which were highly similar to the corresponding proteins in VanA and VanB types of resistance. The deduced VanYD protein was homologous to penicillin-binding proteins that display DD-carboxypeptidase activity. The 5' end coded for the putative VanRD-VanSD two-component regulatory system. Due to a frameshift mutation in the chromosomal ddl gene, BM4339 produced an impaired D-alanine:D-alanine ligase. However, since expression of the resistance genes is constitutive, growth of E. faecium BM4339 was not dependent on the presence of glycopeptides in the culture medium.

* Corresponding author. Mailing address: Unité des Agents Antibactériens, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: (33) 1 45 68 83 20. Fax: (33) 1 45 68 83 19. E-mail: pcourval{at}pasteur.fr.

Journal of Bacteriology, June 1999, p. 3644-3648, Vol. 181, No. 12
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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