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Updated: Jul 7, 2026

The Use of a β-lactamase-based Conductimetric Biosensor Assay to Detect Biomolecular Interactions
Published on: February 1, 2018
Penicillin-binding proteins and beta-lactam resistance.
André Zapun1, Carlos Contreras-Martel, Thierry Vernet
1Laboratoire d'Ingénierie des Macromolécules, Institut de Biologie Structurale Jean-Pierre Ebel, UMR 5075-CNRS, CEA, Université Joseph Fourier, Grenoble, France.
Eubacteria combat beta-lactam antibiotics by evolving low-affinity penicillin-binding proteins (PBPs). Various strategies, including acquiring new PBPs or altering existing ones, enable resistance.
Area of Science:
- Microbiology
- Molecular Biology
- Drug Resistance
Background:
- Eubacteria frequently develop resistance to beta-lactam antibiotics.
- A significant mechanism of resistance involves modifying antibiotic targets.
- Penicillin-binding proteins (PBPs) are crucial targets for beta-lactams.
Purpose of the Study:
- To review the diverse strategies employed by pathogenic eubacteria to resist beta-lactam antibiotics.
- To focus specifically on resistance mechanisms involving low-affinity penicillin-binding proteins (PBPs).
Main Methods:
- Literature review of scientific publications.
- Analysis of documented resistance mechanisms in eubacteria.
- Categorization of strategies based on PBP modification.
Main Results:
- Pathogens utilize several strategies to evade beta-lactams via PBPs.
- These include acquiring novel low-affinity PBPs.
- Endogenous PBPs can be overexpressed or altered via mutations or recombination.
Conclusions:
- Low-affinity PBPs are a versatile target for bacterial resistance to beta-lactams.
- Multiple genetic and regulatory mechanisms contribute to PBP-mediated resistance.
- Understanding these strategies is vital for developing new antibiotics.
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