ArticleACS chemical biology2017
Novel Electrophilic Scaffold for Imaging of Essential Penicillin-Binding Proteins in Streptococcus pneumoniae.
Article in ACS chemical biology, 2017. 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, 33 citations in OpenAlex.
- Structural and Dynamics Analyses of β-Lactam Inhibition ofACS chemical biology · 2026Article
- Decoding the Penicillin-Binding Proteins with Activity-Based Probes.Accounts of chemical research · 2025Review
- Penicillin-binding protein redundancy inApplied and environmental microbiology · 2024Article
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Strategies for Competitive Activity-Based Protein Profiling in Small Molecule Inhibitor Discovery and Characterization.Israel journal of chemistry · 2023Article
- Combined Structural Analysis and Molecular Dynamics Reveal Penicillin-Binding Protein Inhibition Mode with β-Lactones.ACS chemical biology · 2022Article
- Live-Cell Profiling of Penicillin-Binding Protein Inhibitors inACS infectious diseases · 2022Article
- Laponite-Based Nanomaterials for Drug Delivery.Advanced healthcare materials · 2022Review
- Expanded profiling ofBiological chemistry · 2022Article
- Organization of peptidoglycan synthesis in nodes and separate rings at different stages of cell division of Streptococcus pneumoniae.Molecular microbiology · 2021Article
- 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
- Strategies for Tuning the Selectivity of Chemical Probes that Target Serine Hydrolases.Cell chemical biology · 2020Review
- Enzyme-targeted fluorescent small-molecule probes for bacterial imaging.Current opinion in chemical biology · 2020Review
- Harnessing β-Lactam Antibiotics for Illumination of the Activity of Penicillin-Binding Proteins inACS chemical biology · 2020Article
- Activity-based protein profiling in bacteria: Applications for identification of therapeutic targets and characterization of microbial communities.Current opinion in chemical biology · 2020Review
- Chemical Reporters for Exploring Microbiology and Microbiota Mechanisms.Chembiochem : a European journal of chemical biology · 2020Review
- Chemical tools for selective activity profiling of bacterial penicillin-binding proteins.Methods in enzymology · 2020Article
- Chemical tools to characterize peptidoglycan synthases.Current opinion in chemical biology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Peptidoglycan (PG) is a mesh-like heteropolymer made up of glycan chains cross-linked by short peptides and is the major scaffold of eubacterial cell walls, determining cell shape, size, and chaining. This structure, which is required for growth and survival, is located outside of the cytoplasmic membrane of bacterial cells, making it highly accessible to antibiotics. Penicillin-binding proteins (PBPs) are essential for construction of PG and perform transglycosylase activities to generate the glycan strands and transpeptidation to cross-link the appended peptides. The β-lactam antibiotics, which are among the most clinically effective antibiotics for the treatment of bacterial infections, inhibit PBP transpeptidation, ultimately leading to cell lysis. Despite this importance, the discrete functions of individual PBP homologues have been difficult to determine. These major gaps in understanding of PBP activation and macromolecular interactions largely result from a lack of tools to assess the functional state of specific PBPs in bacterial cells. We have identified β-lactones as a privileged scaffold for the generation of PBP-selective probes and utilized these compounds for imaging of the essential proteins, PBP2x and PBP2b, in Streptococcus pneumoniae. We demonstrated that while PBP2b activity is restricted to a ring surrounding the division sites, PBP2x activity is present both at the septal center and at the surrounding ring. These spatially separate regions of PBP2x activity could not be detected by previous activity-based approaches, which highlights a critical strength of our PBP-selective imaging strategy.
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Registered trials
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.