Factors essential for L,D-transpeptidase-mediated peptidoglycan cross-linking and β-lactam resistance in
In: eLife, Jg. 5 (2016-07-08)
Online
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Zugriff:
The target of β-lactam antibiotics is the D,D-transpeptidase activity of penicillin-binding proteins (PBPs) for synthesis of 4→3 cross-links in the peptidoglycan of bacterial cell walls. Unusual 3→3 cross-links formed by L,D-transpeptidases were first detected in Escherichia coli more than four decades ago, however no phenotype has previously been associated with their synthesis. Here we show that production of the L,D-transpeptidase YcbB in combination with elevated synthesis of the (p)ppGpp alarmone by RelA lead to full bypass of the D,D-transpeptidase activity of PBPs and to broad-spectrum β-lactam resistance. Production of YcbB was therefore sufficient to switch the role of (p)ppGpp from antibiotic tolerance to high-level β-lactam resistance. This observation identifies a new mode of peptidoglycan polymerization in E. coli that relies on an unexpectedly small number of enzyme activities comprising the glycosyltransferase activity of class A PBP1b and the D,D-carboxypeptidase activity of DacA in addition to the L,D-transpeptidase activity of YcbB. DOI: http://dx.doi.org/10.7554/eLife.19469.001
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Factors essential for L,D-transpeptidase-mediated peptidoglycan cross-linking and β-lactam resistance in
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Autor/in / Beteiligte Person: | Jean-Emmanuel, Hugonnet ; Dominique, Mengin-Lecreulx ; Alejandro, Monton ; Tanneke, den Blaauwen ; Etienne, Carbonnelle ; Carole, Veckerlé ; Yves V, Brun ; Michael, van Nieuwenhze ; Christiane, Bouchier ; Kuyek, Tu ; Louis B, Rice ; Michel, Arthur |
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Zeitschrift: | eLife, Jg. 5 (2016-07-08) |
Veröffentlichung: | 2016 |
Medientyp: | unknown |
ISSN: | 2050-084X (print) |
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