Characterization of the vanD Glycopeptide Resistance Gene Cluster from Enterococcus faecium BM4339
AUTOR(ES)
Casadewall, Barbara
FONTE
American Society for Microbiology
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=93839Documentos Relacionados
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