A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis.
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 p...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS Pathogens |
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22438804/pdf/?tool=EBI |
| _version_ | 1818722558700158976 |
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| author | Ana Amoroso Julien Boudet Stéphanie Berzigotti Valérie Duval Nathalie Teller Dominique Mengin-Lecreulx André Luxen Jean-Pierre Simorre Bernard Joris |
| author_facet | Ana Amoroso Julien Boudet Stéphanie Berzigotti Valérie Duval Nathalie Teller Dominique Mengin-Lecreulx André Luxen Jean-Pierre Simorre Bernard Joris |
| author_sort | Ana Amoroso |
| collection | DOAJ |
| description | 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 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 β-lactam-resistance factor. The new model proposed confirms and emphasizes the role of peptidoglycan degradation fragments in bacterial cell regulation. |
| first_indexed | 2024-12-17T20:56:32Z |
| format | Article |
| id | doaj.art-da1ae7cc0fa5464291959832d8779d50 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-17T20:56:32Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-da1ae7cc0fa5464291959832d8779d502022-12-21T21:32:51ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742012-01-0183e100257110.1371/journal.ppat.1002571A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis.Ana AmorosoJulien BoudetStéphanie BerzigottiValérie DuvalNathalie TellerDominique Mengin-LecreulxAndré LuxenJean-Pierre SimorreBernard JorisTo 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 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 β-lactam-resistance factor. The new model proposed confirms and emphasizes the role of peptidoglycan degradation fragments in bacterial cell regulation.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22438804/pdf/?tool=EBI |
| spellingShingle | Ana Amoroso Julien Boudet Stéphanie Berzigotti Valérie Duval Nathalie Teller Dominique Mengin-Lecreulx André Luxen Jean-Pierre Simorre Bernard Joris A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis. PLoS Pathogens |
| title | A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis. |
| title_full | A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis. |
| title_fullStr | A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis. |
| title_full_unstemmed | A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis. |
| title_short | A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis. |
| title_sort | peptidoglycan fragment triggers β lactam resistance in bacillus licheniformis |
| url | https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22438804/pdf/?tool=EBI |
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