PMID: 8611145Feb 1, 1996Paper

Peptidoglycan structure of Enterococcus faecium expressing vancomycin resistance of the VanB type

The Biochemical Journal
D Billot-KleinL Gutmann

Abstract

Resistance to glycopeptide antibiotics in enterococci is due to the synthesis of UDP-MurNAc-tetrapeptide-D-lactate (where Mur is muramic acid) replacing the normal UDP-MurNAc-pentapeptide precursor. The peptidoglycan structures of an inducible VanB-type glycopeptide-resistant Enterococcus faecium, D366, and its constitutively resistant derivative, MT9, were determined. Using HPLC, 17 muropeptides were identified and were present regardless of whether resistance was expressed or not. The structures of 15 muropeptides were determined using MS and amino acid analysis. The cross-bridge between D-alanine and L-lysine consisted of one asparagine. No monomer pentapeptide or tetrapeptide-D-lactate could be identified. These results obtained with D366 (non-induced) and MT9 indicate that, in the absence of vancomycin, the cell wall synthetic machinery of E. faecium can process the lactate-containing precursor as efficiently as the normal pentapeptide. In contrast, the presence of subinhibitory inducing concentrations of vancomycin interfered with the synthesis of oligomers.

Citations

Jul 7, 2009·Journal of Molecular Biology·Gary J PattiJacob Schaefer
Jun 8, 2010·The Journal of Biological Chemistry·Marie DeghorainPascal Hols
May 11, 2000·Proceedings of the National Academy of Sciences of the United States of America·J van Heijenoort, L Gutmann
Apr 5, 2000·The Journal of Biological Chemistry·J L MainardiL Gutmann
Dec 8, 2007·Microbiology and Molecular Biology Reviews : MMBR·Jean van Heijenoort
Jun 22, 2002·The Journal of Biological Chemistry·Jean-Luc MainardiLaurent Gutmann
Dec 26, 2006·Journal of Food Protection·Stéphane Caillet, Monique Lacroix
Feb 5, 2014·Journal of Chemical Information and Modeling·Diane Joseph-McCarthyDemetri Moustakas

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