Characterization of the vanD Glycopeptide Resistance Gene Cluster from Enterococcus faecium BM4339
| Autor: | Barbara Casadewall, P Courvalin |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Genotype
Enterococcus faecium Molecular Sequence Data Genetics and Molecular Biology Carboxypeptidases Biology Microbiology Frameshift mutation Open Reading Frames Plasmid Bacterial Proteins Vancomycin Gene cluster Escherichia coli Amino Acid Sequence Peptide Synthases Frameshift Mutation Molecular Biology Peptide sequence Gene Conserved Sequence chemistry.chemical_classification Genetics DNA ligase Base Sequence Membrane Proteins Drug Resistance Microbial biochemical phenomena metabolism and nutrition Chromosomes Bacterial biology.organism_classification Molecular biology Streptomyces Glycopeptide Anti-Bacterial Agents chemistry Multigene Family Sequence Alignment Plasmids |
| Zdroj: | Journal of Bacteriology. 181:3644-3648 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.181.12.3644-3648.1999 |
| Popis: | 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 VanH D dehydrogenase, the VanD ligase, and the VanX D dd -dipeptidase, which were highly similar to the corresponding proteins in VanA and VanB types of resistance. The deduced VanY D protein was homologous to penicillin-binding proteins that display dd -carboxypeptidase activity. The 5′ end coded for the putative VanR D -VanS D 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. |
| Databáze: | OpenAIRE |
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