ArticlemSphere2022
Penicillin Binding Proteins and β-Lactamases of Mycobacterium tuberculosis: Reexamination of the Historical Paradigm.
Article in mSphere, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Synthesis of 4-Aminoindole-Containing Cephalosporin Prodrugs and Their Biological Activity againstACS infectious diseases · 2026Article
- Loss-of-Function Mutations in the Penicillin-Binding Protein PonA1 Confer Agar-Dependent Resistance to Durlobactam inAntibiotics (Basel, Switzerland) · 2025Article
- Targeting mycobacterial transpeptidases: evaluating the roles of Ldt and PBP inhibition in suppressingAntimicrobial agents and chemotherapy · 2025Article
- Combinations comprising dual β-lactams and a β-lactamase inhibitor achieve optimal synergistic inhibition ofAntimicrobial agents and chemotherapy · 2025Article
- Comparative evaluation of five β-Lactamase inhibitors in combination with β-Lactams against multidrug-resistant Mycobacterium tuberculosis in vitro.BMC infectious diseases · 2025Article
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- Progress of anti-tuberculosis drug targets and novel therapeutic strategies.Frontiers in microbiology · 2025Review
- Breaking barriers: The potential of nanosystems in antituberculosis therapy.Bioactive materials · 2024Review
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- The MSMEG_1586 of M. smegmatis Is a Penicillin-Interactive Enzyme That Can Potentially Hydrolyse Aztreonam and Cephalosporins.Current microbiology · 2023Article
- Chemical genetic approaches for the discovery of bacterial cell wall inhibitors.RSC medicinal chemistry · 2023Review
- Structural insights into RNase J that plays an essential role in Mycobacterium tuberculosis RNA metabolism.Nature communications · 2023Article
- Repurposing β-Lactams for the Treatment ofAntibiotics (Basel, Switzerland) · 2023Article
- Challenges & Solutions for Recent Advancements in Multi-Drugs Resistance Tuberculosis: A Review.Microbiology insights · 2023Review
- Tuberculosis treatment failure associated with evolution of antibiotic resilience.Science (New York, N.Y.) · 2022Article
- Clofazimine as a comparator for preclinical efficacy evaluations of experimental therapeutics against pulmonary M. abscessus infection in mice.Tuberculosis (Edinburgh, Scotland) · 2022Article
- Structure-Activity Relationship of Penem Antibiotic Side Chains Used against Mycobacteria Reveals Highly Active Compounds.ACS infectious diseases · 2022Article
- T405, a New Penem, ExhibitsAntimicrobial agents and chemotherapy · 2022Article
- Identification of drivers of mycobacterial resistance to peptidoglycan synthesis inhibitors.Frontiers in microbiology · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Penicillin binding proteins (PBPs) have been extensively studied due to their importance to the physiology of bacterial cell wall peptidoglycan and as targets of the most widely used class of antibiotics, the β-lactams. The existing paradigm asserts that PBPs catalyze the final step of peptidoglycan biosynthesis, and β-lactams inhibit their activities. According to this paradigm, a distinct enzyme class, β-lactamases, exists to inactivate β-lactams. This paradigm has been the basis for how bacterial diseases are treated with β-lactams. We tested whether this historical view accurately reflects the relationship between β-lactams and the PBPs and the β-lactamase, BlaC, of Mycobacterium tuberculosis. BlaC was the major inactivator of the cephalosporin subclass of β-lactams. However, the PBPs PonA1 and PonA2 inactivated penicillins and carbapenems more effectively than BlaC. These findings demonstrate that select M. tuberculosis PBPs are effective at inactivating several β-lactams. Lesser-known PBPs, DacB, DacB1, DacB2, and Rv2864c, a putative PBP, were comparably more resistant to inhibition by all β-lactam subclasses. Additionally, Rv1730c exhibited low affinity to most β-lactams. Based on these findings, we conclude that in M. tuberculosis, BlaC is not the only source of inactivation of β-lactams. Therefore, the historical paradigm does not accurately describe the relationship between β-lactams and M. tuberculosis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.