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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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