ArticleNature chemical biology2022
Autoinducer-fluorophore conjugates enable FRET in LuxR proteins in vitro and in cells.
Article in Nature chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Discovery of dietary polyphenols targeting the autoinducer-2 quorum sensing system of pathogenic bacteria.Gut microbes · 2026Article
- Domain-Swapped LuxR-Type Quorum Sensing Receptors Reveal Divergent Ligand-Response Mechanisms among Homologues.Journal of the American Chemical Society · 2026Article
- Quorum Sensing and Quorum Quenching in Pseudomonas aeruginosa and Staphylococcus aureus Infections: Therapeutic Potential, Limitations and Clinical Challenges.Antibiotics (Basel, Switzerland) · 2026Review
- Bioinformatics-Driven, Plant-Based Antibiotic Research Against Quorum Sensing and Biofilm Formation inBiomolecules · 2026Review
- Chemical Probes that Target a Dissociative LuxR-Type Quorum Sensing Receptor in Gram-Negative Bacteria.ACS chemical biology · 2025Article
- Sulfonyl Homoserine Lactones Are Tunable Probes to Inhibit the Quorum Sensing Receptor RhlR and Reduce Swarming Motility inACS infectious diseases · 2025Article
- Insights into the Mechanisms of Small Molecule-Induced Agonism and Antagonism of a Quorum Sensing Receptor inJournal of the American Chemical Society · 2025Article
- Mucous Permeable Nanoparticle for Inducing Cuproptosis-Like Death In Broad-Spectrum Bacteria for Nebulized Treatment of Acute Pneumonia.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Silyl-Lipid FunctionalizedACS chemical biology · 2025Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Cell-to-cell signaling, or quorum sensing (QS), in many Gram-negative bacteria is governed by small molecule signals (N-acyl-L-homoserine lactones, AHLs) and their cognate receptors (LuxR-type proteins). The mechanistic underpinnings of QS in these bacteria are severely limited due to the challenges of isolating and manipulating most LuxR-type proteins. Reports of quantitative direct-binding experiments on LuxR-type proteins are scarce, and robust and generalizable methods that provide such data are largely nonexistent. We report herein a Förster resonance energy transfer (FRET) assay that leverages (1) conserved tryptophans located in the LuxR-type protein ligand-binding site and synthetic fluorophore-AHL conjugates, and (2) isolation of the proteins bound to weak agonists. The FRET assay permits straightforward measurement of ligand-binding affinities with receptor-either in vitro or in cells-and was shown to be compatible with six LuxR-type proteins. These methods will advance fundamental investigations of LuxR-type protein mechanism and the development of small molecule QS modulators.
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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.