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Structural identification of a bacterial quorum-sensing signal containing boron

Author

Listed:
  • Xin Chen

    (Princeton University)

  • Stephan Schauder

    (Princeton University)

  • Noelle Potier

    (Laboratoire de Spectrometrie de Masse Bio-Organique, Ecole de Chimie, Polymeres et Materiaux)

  • Alain Van Dorsselaer

    (Laboratoire de Spectrometrie de Masse Bio-Organique, Ecole de Chimie, Polymeres et Materiaux)

  • István Pelczer

    (Princeton University)

  • Bonnie L. Bassler

    (Princeton University)

  • Frederick M. Hughson

    (Princeton University)

Abstract

Cell–cell communication in bacteria is accomplished through the exchange of extracellular signalling molecules called autoinducers. This process, termed quorum sensing, allows bacterial populations to coordinate gene expression. Community cooperation probably enhances the effectiveness of processes such as bioluminescence, virulence factor expression, antibiotic production and biofilm development1,2,3,4. Unlike other autoinducers, which are specific to a particular species of bacteria, a recently discovered autoinducer (AI-2)5 is produced by a large number of bacterial species. AI-2 has been proposed to serve as a ‘universal’ signal for inter-species communication1,2,6,7. The chemical identity of AI-2 has, however, proved elusive. Here we present the crystal structure of an AI-2 sensor protein, LuxP, in a complex with autoinducer. The bound ligand is a furanosyl borate diester that bears no resemblance to previously characterized autoinducers. Our findings suggest that addition of naturally occurring borate to an AI-2 precursor generates active AI-2. Furthermore, they indicate a potential biological role for boron, an element required by a number of organisms but for unknown reasons.

Suggested Citation

  • Xin Chen & Stephan Schauder & Noelle Potier & Alain Van Dorsselaer & István Pelczer & Bonnie L. Bassler & Frederick M. Hughson, 2002. "Structural identification of a bacterial quorum-sensing signal containing boron," Nature, Nature, vol. 415(6871), pages 545-549, January.
  • Handle: RePEc:nat:nature:v:415:y:2002:i:6871:d:10.1038_415545a
    DOI: 10.1038/415545a
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    Cited by:

    1. Lei Liao & Bin Chen & Kaikai Deng & Qiang He & Guijiao Lin & Jinsong Guo & Peng Yan, 2023. "Effect of the N-hexanoyl-L-homoserine Lactone on the Carbon Fixation Capacity of the Algae–Bacteria System," IJERPH, MDPI, vol. 20(6), pages 1-14, March.
    2. G.R. Dixon, 2002. "Interactions of soil nutrient environment, pathogenesis and host resistance," Plant Protection Science, Czech Academy of Agricultural Sciences, vol. 38(SI1-6thCo), pages 87-94.
    3. Randy Hamchand & Kevin Wang & Deguang Song & Noah W. Palm & Jason M. Crawford, 2024. "Mucosal sugars delineate pyrazine vs pyrazinone autoinducer signaling in Klebsiella oxytoca," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    4. Andréia Bergamo Estrela & Wolf-Rainer Abraham, 2016. "Fungal Metabolites for the Control of Biofilm Infections," Agriculture, MDPI, vol. 6(3), pages 1-26, August.

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