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A more recent version of this article appeared on November 18, 2005
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M507384200v1
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Papers In Press, published online ahead of print September 6, 2005
J. Biol. Chem, 10.1074/jbc.M507384200
Submitted on July 7, 2005
Revised on September 1, 2005
Accepted on September 6, 2005

A novel peptidoglycan cross-linking enzyme for a beta -lactam-resistant transpeptidation pathway

Jean-Luc Mainardi, Martine Fourgeaud, Jean-Emmanuel Hugonnet, Lionel Dubost, Jean-Paul Brouard, Jamal Ouazzani, Louis B. Rice, Laurent Gutmann, and Michel Arthur

INSERM U655-LRMA, Universite Pierre et Marie Curie (UPMC-Paris 6), Paris, Cedex 06 75270

Corresponding Author: jlmainar{at}bhdc.jussieu.fr

The beta -lactam antibiotics remain the most commonly used to treat severe infections. Due to structural similarity between the beta -lactam ring and the D-alanyl4-D-alanine5 extremity of bacterial cell wall precursors, the drugs act as suicide substrates of the D,D-transpeptidases which catalyze the last cross-linking step of cell wall assembly. Here, we show that this mechanism of action can be defeated by a novel type of transpeptidase identified for the first time by reverse genetics in a beta -lactam-resistant mutant of Enterococcus faecium. The enzyme, Ldtfm, catalyzes in vitro the cross-linking of peptidoglycan subunits in a beta -lactam-insensitive L,D-transpeptidation reaction. The specificity of Ldtfmfor the L-lysyl3-D-alanine4 peptide bond of tetrapeptide donors accounts for resistance since the substrate does not mimic beta -lactams in contrast to D-alanyl4-D-alanine5in the pentapeptide donors required for D,D-transpeptidation. Ldtfmhomologues are encountered sporadically among taxonomically distant bacteria, indicating that L,D-transpeptidase-mediated resistance may emerge in various pathogens.


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