Penicillin-binding proteins (PBPs) are the targets of -lactam antibiotics. These enzymes catalyze the last stages in the polymerization of peptidoglycan, the major constituent of the cell wall. The peptidoglycan, or murein, is a giant molecule, which forms a molecular mesh around the plasma membrane. Chains of tandemly repeated disaccharides form the glycan strands that are linked to each other by short peptide bridges. The discoveries of the PBPs and their cross-bridging mechanism were intimately intertwined. On the basis of studies of the effect of penicillin on peptidoglycan synthesis, it was concluded that cross-linking of the glycan chains resulted from a transpeptidation reaction, which is inhibited by -lactams (1, 2). The fi rst PBPs were isolated a few years later by covalent affi nity chromatography on penicillin- substituted resin (3). Some of these PBPs were dd- carboxypeptidases or endopeptidases rather than transpeptidases. In the intervening three decades, intense research has been carried out on PBPs, particularly on their role in the resistance to -lactams of some important pathogens such as Staphylococcus aureus, Enterococci and Streptococcus pneumoniae.
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Keywords
- Streptococcus Pneumoniae
- Antimicrob Agent
- Neisseria Gonorrhoeae
- Methicillin Resistance
- Penicillin Resistance
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Zapun, A., Macheboeuf, P., Vernet, T. (2009). Penicillin-Binding Proteins and β-Lactam Resistance. In: Mayers, D.L. (eds) Antimicrobial Drug Resistance. Infectious Disease. Humana Press. https://doi.org/10.1007/978-1-59745-180-2_13
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