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J Biol Chem, Vol. 274, Issue 27, 18942-18946, July 2, 1999
From The Rockefeller University, New York, New York 10021
Both vancomycin- and teicoplanin-resistant
laboratory mutants of Staphylococcus aureus produce
peptidoglycans of altered composition in which the proportion of highly
cross-linked muropeptide species is drastically reduced with a parallel
increase in the representation of muropeptide monomers and
dimers (Sieradzki, K., and Tomasz, A. (1997) J. Bacteriol. 179, 2557-2566; and Sieradzki, K., and Tomasz, A. (1998) Microb. Drug Resist. 4, 159-168). We now report that the distorted peptidoglycan composition is related to defects in
penicillin-binding protein 4 (PBP4); no PBP4 was detectable by the
fluorographic assay in membrane preparations from the mutants, and
comparison of the sequence of pbp4 amplified from the
mutants indicated disruption of the gene by two types of abnormalities, a 17-amino acid long duplication starting at position 305 of the pbp4 gene was detected in the vancomycin-resistant mutant,
and a stop codon was found to be introduced into the pbp4
KTG motif at position 261 in the mutant selected for teicoplanin
resistance. Additional common patterns of disturbances in the
peptidoglycan metabolism of the mutants are indicated by the increased
sensitivity of mutant cell walls to the M1 muramidase and decreased
sensitivity to lysostaphin, which is a reversal of the susceptibility
pattern of the parental cell walls. Furthermore, the results of high
performance liquid chromatography analysis of lysostaphin digests of
peptidoglycan suggest an increase in the average chain length of the
glycan strands in the peptidoglycan of the glycopeptide-resistant
mutants. The increased molar proportion of muropeptide monomers in the cell wall of the glycopeptide-resistant mutants should provide binding
sites for the "capture" of vancomycin and teicoplanin molecules,
which may be part of the mechanism of glycopeptide resistance in
S. aureus.
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