VanD-type glycopeptide-resistant Enterococcus faecium BM4339 | Zendy

Bruno Périchon | Zendy; Peter E. Reynolds | Zendy; Patrice Courvalin | Zendy

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VanD-type glycopeptide-resistant Enterococcus faecium BM4339

Author(s) -

Bruno Périchon,

Peter E. Reynolds,

Patrice Courvalin

Publication year - 1997

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.41.9.2016

Subject(s) - glycopeptide , teicoplanin , enterococcus faecium , microbiology and biotechnology , biology , enterococcus , vancomycin , peptidoglycan , glycopeptide antibiotic , cloning (programming) , biochemistry , gene , genetics , bacteria , antibiotics , staphylococcus aureus , computer science , programming language

Enterococcus faecium BM4339 was constitutively resistant to vancomycin (MIC, 64 microg/ml) and to low levels of teicoplanin (MIC, 4 microg/ml). A 605-bp product obtained with the V1 and V2 primers for amplification of genes encoding D-Ala:D-Ala ligases and related glycopeptide resistance proteins was sequenced after cloning. The deduced amino acid sequence had 69% identity with VanA and VanB and 43% identity with VanC, consistent with the finding that BM4339 synthesized peptidoglycan precursors terminating in D-lactate. This new type of glycopeptide resistance phenotype was designated VanD.

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