Increased Glycan Chain Length Distribution and Decreased Susceptibility to Moenomycin in a Vancomycin-Resistant Staphylococcus aureus Mutant | Zendy

Hitoshi Komatsuzawa | Zendy; Kouji Ohta | Zendy; Sakuo Yamada | Zendy; Kerstin Ehlert | Zendy; Harald Labischinski | Zendy; Junko Kajimura | Zendy; Tamaki Fujiwara | Zendy; Motoyuki Sugai | Zendy

Open Access

Increased Glycan Chain Length Distribution and Decreased Susceptibility to Moenomycin in a Vancomycin-Resistant Staphylococcus aureus Mutant

Author(s) -

Hitoshi Komatsuzawa,

Kouji Ohta,

Sakuo Yamada,

Kerstin Ehlert,

Harald Labischinski,

Junko Kajimura,

Tamaki Fujiwara,

Motoyuki Sugai

Publication year - 2002

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.46.1.75-81.2002

Subject(s) - staphylococcus aureus , glycan , penicillin binding proteins , peptidoglycan , glycopeptide , mutant , vancomycin , microbiology and biotechnology , teicoplanin , penicillin , lysis , biochemistry , chemistry , biology , peptide , cell wall , antibiotics , bacteria , glycoprotein , gene , genetics

A vancomycin-resistant Staphylococcus aureus mutant, COL-VR1 (MIC, 16 microg/ml), was isolated from methicillin-resistant S. aureus COL by exposure to vancomycin. COL-VR1 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.

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