ArticleMethods in enzymology2020
Chemical tools for selective activity profiling of bacterial penicillin-binding proteins.
Article in Methods in enzymology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Antibiotic-Induced Bacterial Cell Death: A "Radical" Way of Dying?Current topics in microbiology and immunology · 2025Article
- Decoding the Penicillin-Binding Proteins with Activity-Based Probes.Accounts of chemical research · 2025Review
- Comprehensive Approaches to CombattingAntibiotics (Basel, Switzerland) · 2024Review
- Structural Insights into the Penicillin-Binding Protein 4 (DacB) fromInternational journal of molecular sciences · 2024Article
- Electrochemical Affinity Biosensors: Pervasive Devices with Exciting Alliances and Horizons Ahead.ACS sensors · 2023Review
- β-Lactams from the Ocean.Marine drugs · 2023Review
- Identification of Bacteria Associated with Post-Operative Wounds of Patients with the Use of Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry Approach.Molecules (Basel, Switzerland) · 2021Article
- Organization of peptidoglycan synthesis in nodes and separate rings at different stages of cell division of Streptococcus pneumoniae.Molecular microbiology · 2021Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Comparison of Bioorthogonal β-Lactone Activity-Based Probes for Selective Labeling of Penicillin-Binding Proteins.Chembiochem : a European journal of chemical biology · 2021Article
- The Pneumococcal Divisome: Dynamic Control ofFrontiers in microbiology · 2021Review
- From Differential Stains to Next Generation Physiology: Chemical Probes to Visualize Bacterial Cell Structure and Physiology.Molecules (Basel, Switzerland) · 2020Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Penicillin-binding proteins (PBPs) are membrane-associated proteins involved in the biosynthesis of peptidoglycan (PG), the main component of bacterial cell walls. These proteins were discovered and named for their affinity to bind the β-lactam antibiotic penicillin. The importance of the PBPs has long been appreciated; however, specific roles of individual family members in each bacterial strain, as well as their protein-protein interactions, are yet to be understood. The apparent functional redundancy of the 4-18 PBPs that most eubacteria possess makes determination of their individual roles difficult. Existing techniques to study PBPs are not ideal because they do not directly visualize protein activity and can suffer from artifacts and perturbations of native PBP function. Therefore, development of new methods for studying the roles of individual PBPs in cell wall synthesis is required. We recently generated a library of fluorescent chemical probes containing a β-lactone scaffold that specifically targets the PBPs, enabling the visualization of their catalytic activity. Herein, we describe a general protocol to label and detect the activity of individual PBPs in Streptococcus pneumoniae using our fluorescent β-lactone probes.
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