ArticleNature communications2022
Moonlighting chaperone activity of the enzyme PqsE contributes to RhlR-controlled virulence of Pseudomonas aeruginosa.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- A quorum sensing antagonist with dual bacterium- and host-directed anti-pathogenic activity againstVirulence · 2026Article
- MrtR ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Domain-Swapped LuxR-Type Quorum Sensing Receptors Reveal Divergent Ligand-Response Mechanisms among Homologues.Journal of the American Chemical Society · 2026Article
- Coumarins Disrupt Cell-Cell Communication and Virulence in Priority Pathogens: Targeting the PQS Signalling System in Pseudomonas aeruginosa.Microbial biotechnology · 2026Article
- Quorum sensing inhibition strategies for the control of Pseudomonas aeruginosa infections.World journal of microbiology & biotechnology · 2026Review
- New inhibitors of themSphere · 2026Article
- The conserved coordination of acyl-homoserine lactone and PqsE signaling defines the RhlR-dependent quorum-sensing network inbioRxiv : the preprint server for biology · 2026Article
- RhlR quorum-sensing receptor ligand sensitivity regulates the differential expression of phenazine genes inJournal of bacteriology · 2026Article
- The post-translational adaptor protein SadB modulates the pathogenicity ofJournal of bacteriology · 2026Article
- Role of PsrA in physiology and virulence regulation inJournal of bacteriology · 2026Review
- The nucleoid-associated protein subunit HupA positively regulates the Pqs system and pyocyanin production inApplied and environmental microbiology · 2026Article
- Expanding the LuxR-type receptor functional repertoire: Protein-protein interactions in quorum sensing regulation.PLoS pathogens · 2026Review
- Screening of FDA-Approved Small Molecules to Discover Inhibitors of theBiochemistry · 2026Article
- Regulation of interbacterial interactions betweenbioRxiv : the preprint server for biology · 2026Article
- Conserved differential expression of DDX helicase and CPEB genes in skeletal muscles potentially influences neuromuscular junctions during aging: a computational analysis.Biogerontology · 2026Article
- UnderstandingMicroorganisms · 2026Review
- Microbial phenazines: biosynthesis, structural diversity, evolution, regulation, and biological significance.Microbiology and molecular biology reviews : MMBR · 2025Review
- Article
- Multifaceted quorum-sensing inhibiting activity of 3-(Benzo[d][1,3]dioxol-4-yl)oxazolidin-2-one mitigatesVirulence · 2025Article
- PqsE has a conserved sequence, yet a variable impact inJournal of bacteriology · 2025Article
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17 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Pseudomonas aeruginosa is a major cause of nosocomial infections and also leads to severe exacerbations in cystic fibrosis or chronic obstructive pulmonary disease. Three intertwined quorum sensing systems control virulence of P. aeruginosa, with the rhl circuit playing the leading role in late and chronic infections. The majority of traits controlled by rhl transcription factor RhlR depend on PqsE, a dispensable thioesterase in Pseudomonas Quinolone Signal (PQS) biosynthesis that interferes with RhlR through an enigmatic mechanism likely involving direct interaction of both proteins. Here we show that PqsE and RhlR form a 2:2 protein complex that, together with RhlR agonist N-butanoyl-L-homoserine lactone (C4-HSL), solubilizes RhlR and thereby renders the otherwise insoluble transcription factor active. We determine crystal structures of the complex and identify residues essential for the interaction. To corroborate the chaperone-like activity of PqsE, we design stability-optimized variants of RhlR that bypass the need for C4-HSL and PqsE in activating PqsE/RhlR-controlled processes of P. aeruginosa. Together, our data provide insight into the unique regulatory role of PqsE and lay groundwork for developing new P. aeruginosa-specific pharmaceuticals.
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