Unknown

Dataset Information

0

A peptidoglycan fragment triggers ?-lactam resistance in Bacillus licheniformis.


ABSTRACT: To resist to ?-lactam antibiotics Eubacteria either constitutively synthesize a ?-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 ?-lactam and launches a cytoplasmic signal leading to the inactivation of BlaI/MecI repressor, and the synthesis of a ?-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 ?-lactam-resistance factor. The new model proposed confirms and emphasizes the role of peptidoglycan degradation fragments in bacterial cell regulation.

SUBMITTER: Amoroso A 

PROVIDER: S-EPMC3305447 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

altmetric image

Publications

A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis.

Amoroso Ana A   Boudet Julien J   Berzigotti Stéphanie S   Duval Valérie V   Teller Nathalie N   Mengin-Lecreulx Dominique D   Luxen André A   Simorre Jean-Pierre JP   Joris Bernard B  

PLoS pathogens 20120315 3


To resist to β-lactam antibiotics Eubacteria either constitutively synthesize a β-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 β-lactam and launches a cytoplasmic signal leading to the inactivation of BlaI/MecI repressor, and the synthesis of a β-lactamase or a low affini  ...[more]

Similar Datasets

| S-EPMC1168070 | biostudies-other
| S-EPMC3306796 | biostudies-literature
| S-EPMC3697359 | biostudies-literature
| S-EPMC1165295 | biostudies-other
| S-EPMC1166343 | biostudies-other
| S-EPMC7144989 | biostudies-literature
| S-EPMC1161281 | biostudies-other
| S-EPMC6196517 | biostudies-literature
2015-04-21 | PXD000791 | Pride
| S-EPMC4174774 | biostudies-literature