Structural identification of a bacterial quorum-sensing signal containing boron

Xin Chen, Stephan Schauder, Noelle Potier, Alain Van Dorsselaer, István Pelczer, Bonnie L. Bassler and Frederick M. Hughson ()
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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

Nature, 2002, vol. 415, issue 6871, 545-549

Abstract: 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.

Date: 2002
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DOI: 10.1038/415545a

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