ArticleACS chemical biology2019
An Autoinducer Analogue Reveals an Alternative Mode of Ligand Binding for the LasR Quorum-Sensing Receptor.
Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 47 citations in OpenAlex.
- You Talking to Me? Quorum Sensing in Symbiotic Microbes and Their Response to Environmental Variation.Microorganisms · 2026Review
- Combining Triazole Scaffold Repurposing and Generative Transformer Architecture for Structure-Based Inhibitor Design Targeting the LasR Quorum Sensing Receptor ofPharmaceuticals (Basel, Switzerland) · 2026Article
- RhlR quorum-sensing receptor ligand sensitivity regulates the differential expression of phenazine genes inJournal of bacteriology · 2026Article
- Article
- 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
- Silyl-Lipid FunctionalizedACS chemical biology · 2025Article
- Quorum Sensing and its Inhibition inCurrent drug targets · 2025Review
- Abiotic Small Molecule Inhibitors and Activators of the LasR Quorum Sensing Receptor inACS infectious diseases · 2024Article
- Article
- A data-driven machine learning approach for discovering potent LasR inhibitors.Bioengineered · 2023Article
- Norlobaridone Inhibits Quorum Sensing-Dependent Biofilm Formation and Some Virulence Factors inBiomolecules · 2023Article
- A Geneticist Transcribing the Chemical Language of Bacteria.Israel journal of chemistry · 2023Article
- ModifiedFrontiers in molecular biosciences · 2023Article
- Anti-quorum sensing potential of selenium nanoparticles against LasI/R, RhlI/R, and PQS/MvfR inFrontiers in molecular biosciences · 2023Article
- Structure of the RhlR-PqsE complex from Pseudomonas aeruginosa reveals mechanistic insights into quorum-sensing gene regulation.Structure (London, England : 1993) · 2022Article
- Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa.Nature communications · 2022Article
- Resistance Is Not Futile: The Role of Quorum Sensing Plasticity inMicroorganisms · 2022Review
- Cheminformatics analysis of molecular datasets of transcription factors associated with quorum sensing inRSC advances · 2022Article
- The role of eugenol and ferulic acid as the competitive inhibitors of transcriptional regulator RhlR inMethodsX · 2022Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Bacteria use a cell-cell communication process called quorum sensing to coordinate collective behaviors. Quorum sensing relies on production and group-wide detection of extracellular signal molecules called autoinducers. Here, we probe the activity of the Pseudomonas aeruginosa LasR quorum-sensing receptor using synthetic agonists based on the structure of the native homoserine lactone autoinducer. The synthetic compounds range from low to high potency, and agonist activity tracks with the ability of the agonist to stabilize the LasR protein. Structural analyses of the LasR ligand binding domain complexed with representative synthetic agonists reveal two modes of ligand binding, one mimicking the canonical autoinducer binding arrangement, and the other with the lactone head group rotated approximately 150°. Iterative mutagenesis combined with chemical synthesis reveals the amino acid residues and the chemical moieties, respectively, that are key to enabling each mode of binding. Simultaneous alteration of LasR residues Thr75, Tyr93, and Ala127 converts low-potency compounds into high-potency compounds and converts ligands that are nearly inactive into low-potency compounds. These results show that the LasR binding pocket displays significant flexibility in accommodating different ligands. The ability of LasR to bind ligands in different conformations, and in so doing, alter their potency as agonists, could explain the difficulties that have been encountered in the development of competitive LasR inhibitors.
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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.