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A Novel Peptidoglycan Cross-linking Enzyme for a β-Lactam-resistant Transpeptidation Pathway
Open accessAbstract
The beta-lactam antibiotics remain the most commonly used to treat severe infections. Because of structural similarity between the beta-lactam ring and the d-alanyl(4)-d-alanine(5) extremity of bacterial cell wall precursors, the drugs act as suicide substrates of the dd-transpeptidases that catalyze the last cross-linking step of cell wall assembly. Here, we show that this mechanism of action can be defeated by a novel type of transpeptidase identified for the first time by reverse genetics in abeta-lactam-resistant mutant of Enterococcus faecium. The enzyme, Ldt(fm), catalyzes in vitro the cross-linking of peptidoglycan subunits in a beta-lactam-insensitive ld-transpeptidation reaction. The specificity of Ldt(fm) for the l-lysyl(3)-d-alanine(4) peptide bond of tetrapeptide donors accounts for resistance because the substrate does not mimic beta-lactams in contrast to d-alanyl(4)-d-alanine(5) in the pentapeptide donors required for dd-transpeptidation. Ldt(fm) homologues are encountered sporadically among taxonomically distant bacteria, indicating that ld-transpeptidase-mediated resistance may emerge in various pathogens.
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Citations
Cited by
Peptidoglycan structure and architecture
Vollmer, W., Blanot, D., & De Pedro, M. A. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00094.x · Cited by 2,340
Penicillin-binding proteins and β-lactam resistance
Zapun, A., Contreras-Martel, C., & Vernet, T. (2008) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2007.00095.x · Cited by 687
Lavollay, M., Arthur, M., Fourgeaud, M., Dubost, L., Marie, A., Veziris, N., Blanot, D., Gutmann, L., & Mainardi, J.-L. (2008) · Journal of Bacteriology · doi:10.1128/jb.00239-08 · Cited by 349
Self-citationGupta, R., Lavollay, M., Mainardi, J.-L., Arthur, M., Bishai, W. R., & Lamichhane, G. (2010) · Nature Medicine · doi:10.1038/nm.2120 · Cited by 281
Self-citationCopper tolerance in bacteria requires the activation of multiple accessory pathways
Giachino, A., & Waldron, K. J. (2020) · Molecular Microbiology · doi:10.1111/mmi.14522 · Cited by 223
Metadata
- Authors
- Mainardi, J.-L., Fourgeaud, M., Hugonnet, J.-E., Dubost, L., Brouard, J.-P., Ouazzani, J., Rice, L. B., Gutmann, L., & Arthur, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-11
- Volume
- 280
- Issue
- 46
- Pages
- 38146-38152
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2067572953
- Cited by
- 225
- References
- 0
- FWCI
- 2.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: A Novel Peptidoglycan Cross-linking Enzyme for a β-Lactam-resistant Transpeptidation Pathway. https://app.cochat.ai/papers/10.1074/jbc.m507384200
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- Mainardi, J.-L., Fourgeaud, M., Hugonnet, J.-E., Dubost, L., Brouard, J.-P., Ouazzani, J., Rice, L. B., Gutmann, L., & Arthur, M. (2005). A Novel Peptidoglycan Cross-linking Enzyme for a β-Lactam-resistant Transpeptidation Pathway. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m507384200
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