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A strategy for antagonizing quorum sensing.

Chen G, Swem LR, Swem DL, Stauff DL, O'Loughlin CT, Jeffrey PD, Bassler BL, Hughson FM
Mol Cell 42 199-209 (2011)
Related entries: 3qp1, 3qp2, 3qp4, 3qp6, 3qp8

Cited: 152 times
EuropePMC logo PMID: 21504831

Abstract

Quorum-sensing bacteria communicate via small molecules called autoinducers to coordinate collective behaviors. Because quorum sensing controls virulence factor expression in many clinically relevant pathogens, membrane-permeable quorum sensing antagonists that prevent population-wide expression of virulence genes offer a potential route to novel antibacterial therapeutics. Here, we report a strategy for inhibiting quorum-sensing receptors of the widespread LuxR family. Structure-function studies with natural and synthetic ligands demonstrate that the dimeric LuxR-type transcription factor CviR from Chromobacterium violaceum is potently antagonized by molecules that bind in place of the native acylated homoserine lactone autoinducer, provided that they stabilize a closed conformation. In such conformations, each of the two DNA-binding domains interacts with the ligand-binding domain of the opposing monomer. Consequently, the DNA-binding helices are held apart by ∼60 Å, twice the ∼30 Å separation required for operator binding. This approach may represent a general strategy for the inhibition of multidomain proteins.

Reviews - 3qp5 mentioned but not cited (3)

  1. Quorum sensing signal-response systems in Gram-negative bacteria. Papenfort K, Bassler BL. Nat Rev Microbiol 14 576-588 (2016)
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Articles - 3qp5 mentioned but not cited (25)

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Reviews citing this publication (33)

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Articles citing this publication (91)

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