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Antimicrobial Agents and Chemotherapy, January 2001, p. 280-287, Vol. 45, No. 1
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.1.280-287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

A Spectrum of Changes Occurs in Peptidoglycan Composition of Glycopeptide-Intermediate Clinical Staphylococcus aureus Isolates

Susan Boyle-Vavra,1,* Harald Labischinski,2 Christine C. Ebert,1 Kerstin Ehlert,2 and Robert S. Daum1

Department of Pediatrics, University of Chicago, Chicago, Illinois,1 and Bayer AG, Wuppertal, Germany2

Received 12 June 2000/Returned for modification 17 August 2000/Accepted 28 September 2000

The mechanism of glycopeptide resistance in Staphylococcus aureus is not known with certainty. Because the target of vancomycin is the D-Ala-D-Ala terminus of the stem peptide of the peptidoglycan precursor, by subjecting muropeptides to reversed-phase high-performance liquid chromatography, we investigated peptidoglycan obtained from glycopeptide-intermediate S. aureus (GISA) isolates for changes in composition and evaluated whether any peptidoglycan structural change was a consistent feature of clinical GISA isolates. GISA isolates Mu50 and Mu3 from Japan had the large glutamate-containing monomeric peak demonstrated previously, although strain H1, a vancomycin-susceptible MRSA isolate from Japan that was clonally related to Mu3 and Mu50, and a femC mutant that we studied, did also. For the U.S. GISA isolates, strain NJ had a large monomeric peak with a retention time identical to that described for the glutamate-containing monomer in strains H1, Mu3, and Mu50. However, a much smaller corresponding peak was seen in GISA MI, and this peak was absent from both GISA PC and a recent GISA isolate obtained from an adult patient in Illinois (strain IL). These data suggest that a uniform alteration in peptidoglycan composition cannot be discerned among the GISA isolates and indicate that a single genetic or biochemical change is unlikely to account for the glycopeptide resistance phenotype in the clinical GISA isolates observed to date. Furthermore, a large monomeric glutamate-containing peak is not sufficient to confer the resistance phenotype.

* Corresponding author. Mailing address: Department of Pediatrics, University of Chicago, MC 6054, 5841 S. Maryland Ave., Chicago, IL 60637. Phone: (773) 702-6176. Fax: (773) 702-1196. E-mail: sboyleva{at}midway.uchicago.edu.

Antimicrobial Agents and Chemotherapy, January 2001, p. 280-287, Vol. 45, No. 1
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.1.280-287.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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