Reference : A peptidoglycan fragment triggers beta-lactam resistance in Bacillus licheniformis.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
A peptidoglycan fragment triggers beta-lactam resistance in Bacillus licheniformis.
Amoroso, Ana Maria mailto [Université de Liège - ULiège > > Centre d'ingénierie des protéines]
Boudet, Julien [> > > >]
Berzigotti, Stephanie [> > > >]
Duval, Valerie [> > > >]
Teller, Nathalie [> > > >]
Mengin-Lecreulx, Dominique [> > > >]
Luxen, André mailto [Université de Liège - ULiège > Département de chimie (sciences) > Chimie organique de synthèse]
Simorre, Jean*-Pierre [> > > >]
Joris, Bernard mailto [Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes]
PLoS Pathogens
Public Library of Science
Yes (verified by ORBi)
San Francisco
[en] To resist to beta-lactam antibiotics Eubacteria either constitutively synthesize a beta-lactamase or a low affinity penicillin-binding protein target, or induce its synthesis in response to the presence of antibiotic outside the cell. In Bacillus licheniformis and Staphylococcus aureus, a membrane-bound penicillin receptor (BlaR/MecR) detects the presence of beta-lactam and launches a cytoplasmic signal leading to the inactivation of BlaI/MecI repressor, and the synthesis of a beta-lactamase or a low affinity target. We identified a dipeptide, resulting from the peptidoglycan turnover and present in bacterial cytoplasm, which is able to directly bind to the BlaI/MecI repressor and to destabilize the BlaI/MecI-DNA complex. We propose a general model, in which the acylation of BlaR/MecR receptor and the cellular stress induced by the antibiotic, are both necessary to generate a cell wall-derived coactivator responsible for the expression of an inducible beta-lactam-resistance factor. The new model proposed confirms and emphasizes the role of peptidoglycan degradation fragments in bacterial cell regulation.

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