Journal
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
Volume 56, Issue 4, Pages 1877-1884Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.05402-11
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Funding
- REIPI
- Spanish Network for Research in Infectious Diseases (Instituto de Salud Carlos III) [RD06/0008/0025]
- Fondo de Investigaciones Sanitarias [PI061368, PI081368, PS09/00687]
- SERGAS [PS07/90]
- Xunta de Galicia [07CSA050916PR]
- Instituto de Salud Carlos III, Ministerio de Ciencia e Innovacion
- Spanish Society for Microbiology and Infectious Disease (SEIMC)
- Ministry of Science and Innovation (MICINN) [BFU2009-09200]
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beta-Lactamases and penicillin-binding proteins (PBPs) have evolved from a common ancestor. beta-Lactamases are enzymes that degrade beta-lactam antibiotics, whereas PBPs are involved in the synthesis and processing of peptidoglycan, which forms an elastic network in the bacterial cell wall. This study analyzed the interaction between beta-lactamases and peptidoglycan and the impact on fitness and biofilm production. A representative set of all classes of beta-lactamases was cloned in the expression vector pBGS18 under the control of the CTX-M promoter and expressed in Escherichia coli MG1655. The peptidoglycan composition of all clones was evaluated, and quantitative changes were found in E. coli strains expressing OXA-24, OXA-10-like, and SFO-1 (with its upstream regulator AmpR) beta-lactamases; the level of cross-linked muropeptides decreased, and their average length increased. These changes were associated with a statistically significant fitness cost, which was demonstrated in both in vitro and in vivo experiments. The observed changes in peptidoglycan may be explained by the presence of residual DD-endopeptidase activity in these beta-lactamases, which may result in hydrolysis of the peptide cross bridge. The biological cost associated with these changes provides important data regarding the interaction between beta-lactamases and the metabolism of peptidoglycan and may provide an explanation for the epidemiology of these beta-lactamases in Enterobacteriaceae.
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