Increased glycan chain length distribution and decreased susceptibility to moenomycin in a vancomycin-resistant Staphylococcus aureus mutant
Increased glycan chain length distribution and decreased susceptibility to moenomycin in a vancomycin-resistant Staphylococcus aureus mutant
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DOI:
10.1128/aac.46.1.75-81.2002
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发表时间:
2002-01-01
影响因子:
4.9
通讯作者:
Sugai, M
中科院分区:
文献类型:
--
作者:
Komatsuzawa, H;Ohta, K;Sugai, M
A vancomycin-resistant Staphylococcus aureus mutant, COL-VR1 (MIC, 16 mug/ml), was isolated from methicillin-resistant S. aureus COL by exposure to vancomycin. COL-VRI also showed decreased susceptibility to teicoplanin (8-fold), methicillin (2-fold), macarbomycin (8-fold), and moenomycin (16-fold). Macarbomycin and moenomycin are thought to directly inhibit transglycosylase activity. Characterization of the mutant revealed a thickened cell wall and suppression of penicillin-induced lysis, although the amounts of the five penicillin-binding proteins (PBPs 1, 2, 3, 4, and 2') and the profiles of peptidoglycan hydrolases were not altered. Analysis of muropeptide profile and glycan chain length distribution by reversed-phase high-pressure liquid chromatography revealed slightly decreased peptide cross-linking and an increased average glycan chain length compared to those of the parent. These results together suggest that a transglycosylase activity was enhanced in the mutant. This may represent a novel mechanism of glycopeptide resistance in S. aureus.