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Hugonnet, Jean-Emmanuel; Mengin-Lecreulx, Dominique; Monton, Alejandro; den Blaauwen, Tanneke; Carbonnelle, Etienne; Veckerlé, Carole; Brun, Yves V; van Nieuwenhze, Michael; Bouchier, Christiane; Tu, Kuyek; Rice, Louis B; Arthur, Michel
eLife, 10/2016, Letnik: 5Journal Article
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 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 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.
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in: SICRIS
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