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Originally published In Press as doi:10.1074/jbc.M909877199 on March 19, 2000

J. Biol. Chem., Vol. 275, Issue 22, 16490-16496, June 2, 2000
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Novel Mechanism of beta -Lactam Resistance Due to Bypass of DD-Transpeptidation in Enterococcus faecium*

Jean-Luc MainardiDagger §, Raymond Legrand, Michel Arthur||, Bernard Schoot, Jean van Heijenoort||, and Laurent GutmannDagger

From the Dagger  L.R.M.A., UFR Broussais-Hôtel Dieu, Université Paris VI, 75270 Paris, France, the  Physics Department, Hoechst Marion Roussel, Romainville, 93235 France, and the || Biochimie Moléculaire et Cellulaire, CNRS, Orsay, 91405 France

The peptidoglycan structure of in vitro selected ampicillin-resistant mutant Enterococcus faecium D344M512 and of the susceptible parental strain D344S was determined by reverse phase high performance liquid chromatography and mass spectrometry. The muropeptide monomers were almost identical in the two strains. The substantial majority (99.3%) of the oligomers from the susceptible strain D344S contained the usual D-alanyl right-arrow D-asparaginyl (or D-aspartyl)-L-lysyl cross-link (D-Ala right-arrow D-Asx-L-Lys) generated by beta -lactam-sensitive DD-transpeptidation. The remaining oligomers (0.7%) were produced by beta -lactam-insensitive LD-transpeptidation, because they contained L-Lys right-arrow D-Asx-L-Lys cross-links. The muropeptide oligomers of the ampicillin-resistant mutant D344M512 contained only these L-Lys right-arrow D-Asx-L-Lys cross-links indicating that resistance was due to the bypass of the beta -lactam-sensitive DD-transpeptidation reaction. The discovery of this novel resistance mechanism indicates that DD-transpeptidases cannot be considered anymore as the sole essential transpeptidase enzymes.

* This work was supported by Grants CRI 950601 and EHI 0004.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: L.R.M.A., Université Paris VI, 15, rue de l'Ecole de Médecine, 75270 Paris Cedex 06, France. Tel.: 33-1-42-34-68-63; Fax: 33-1-43-25-68-12; E-mail: jlmainar@bhdc.jussieu.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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