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...

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Autores principales:	Ana Amoroso, Julien Boudet, Stéphanie Berzigotti, Valérie Duval, Nathalie Teller, Dominique Mengin-Lecreulx, André Luxen, Jean-Pierre Simorre, Bernard Joris
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/da1ae7cc0fa5464291959832d8779d50
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spelling	oai:doaj.org-article:da1ae7cc0fa5464291959832d8779d502021-11-18T06:04:40ZA peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis.1553-73661553-737410.1371/journal.ppat.1002571https://doaj.org/article/da1ae7cc0fa5464291959832d8779d502012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22438804/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374To 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.Ana AmorosoJulien BoudetStéphanie BerzigottiValérie DuvalNathalie TellerDominique Mengin-LecreulxAndré LuxenJean-Pierre SimorreBernard JorisPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 3, p e1002571 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 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.
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.
format	article
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
title	A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis.
title_short	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_sort	peptidoglycan fragment triggers β-lactam resistance in bacillus licheniformis.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/da1ae7cc0fa5464291959832d8779d50
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A peptidoglycan fragment triggers β-lactam resistance in Bacillus licheniformis.

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