ArticleThe Journal of biological chemistry2017
Substitutions in PBP2b from β-Lactam-resistant
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Penicillin-Binding Proteins inAntibiotics (Basel, Switzerland) · 2026Review
- The effect of MurM and a branched cell wall structure on penicillin resistance inJournal of bacteriology · 2025Article
- Article
- Affinity of cefditoren for penicillin-binding proteins in bacteria and its relationship with antibiotic sensitivity.Archives of microbiology · 2024Article
- Streptococcus suis serotype 9 in Italy: genomic insights into high-risk clones with emerging resistance to penicillin.The Journal of antimicrobial chemotherapy · 2024Article
- Article
- β-Lactam Resistance in Upper Respiratory Tract Pathogens Isolated from a Tertiary Hospital in Malaysia.Pathogens (Basel, Switzerland) · 2021Article
- Large-scale genomic analysis of antimicrobial resistance in the zoonotic pathogen Streptococcus suis.BMC biology · 2021Article
- Comparison of Bioorthogonal β-Lactone Activity-Based Probes for Selective Labeling of Penicillin-Binding Proteins.Chembiochem : a European journal of chemical biology · 2021Article
- Antimicrobial Peptide Designing and Optimization Employing Large-Scale Flexibility Analysis of Protein-Peptide Fragments.ACS omega · 2019Article
- Designing of a penta-peptide against drug resistant E. coli.Bioinformation · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Pneumococcus resists β-lactams by expressing variants of its target enzymes, the penicillin-binding proteins (PBPs), with many amino acid substitutions. Up to 10% of the sequence can be modified. These altered PBPs have a much reduced reactivity with the drugs but retain their physiological activity of cross-linking the peptidoglycan, the major constituent of the bacterial cell wall. However, because β-lactams are chemical and structural mimics of the natural substrate, resistance mediated by altered PBPs raises the following paradox: how PBPs that react poorly with the drugs maintain a sufficient level of activity with the physiological substrate. This question is addressed for the first time in this study, which compares the peptidoglycan cross-linking activity of PBP2b from susceptible and resistant strains with their inhibition by different β-lactams. Unexpectedly, the enzymatic activity of the variants did not correlate with their antibiotic reactivity. This finding indicates that some of the numerous amino acid substitutions were selected to restore a viable level of enzymatic activity by a compensatory molecular mechanism.
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Registered trials
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