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Muropeptides in Pseudomonas aeruginosa and their Role as Elicitors of β‐Lactam‐Antibiotic Resistance
Author(s) -
Lee Mijoon,
Dhar Supurna,
De Benedetti Stefania,
Hesek Dusan,
Boggess Bill,
Blázquez Blas,
Mathee Kalai,
Mobashery Shahriar
Publication year - 2016
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201601693
Subject(s) - pseudomonas aeruginosa , pentapeptide repeat , chemistry , bacteria , antibiotics , cell wall , microbiology and biotechnology , bacterial cell structure , biochemistry , antibiotic resistance , lactam , cell signaling , lipid ii , signal transduction , peptidoglycan , stereochemistry , biology , peptide , genetics
Muropeptides are a group of bacterial natural products generated from the cell wall in the course of its turnover. These compounds are cell‐wall recycling intermediates and are also involved in signaling within the bacterium. However, the identity of these signaling molecules remains elusive. The identification and characterization of 20 muropeptides from Pseudomonas aeruginosa is described. The least abundant of these metabolites is present at 100 and the most abundant at 55,000 molecules per bacterium. Analysis of these muropeptides under conditions of induction of resistance to a β‐lactam antibiotic identified two signaling muropeptides ( N ‐acetylglucosamine‐1,6‐anhydro‐ N ‐acetylmuramyl pentapeptide and 1,6‐anhydro‐ N ‐acetylmuramyl pentapeptide). Authentic synthetic samples of these metabolites were shown to activate expression of β‐lactamase in the absence of any β‐lactam antibiotic, thus indicating that they serve as chemical signals in this complex biochemical pathway.