Structural identification of a bacterial quorum-sensing signal containing boron

• Published in: Nature (London) Vol. 415; no. 6871; pp. 545 - 549
• Main Authors: Hughson, Frederick M, Chen, Xin, Schauder, Stephan, Potier, Noelle, Van Dorsselaer, Alain, Pelczer, István, Bassler, Bonnie L
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 31.01.2002; Nature Publishing Group
• Subjects: Analytical chemistry; autoinducers; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - physiology; Bacteriology; Biofilms; Biological and medical sciences; Bioluminescence; Borates - chemistry; Boron; Boron - chemistry; Boron - physiology; Bridged Bicyclo Compounds, Heterocyclic - chemistry; Cells; Chemical Sciences; Chemistry; Crystallography, X-Ray; Crystals; Escherichia coli; Fundamental and applied biological sciences. Psychology; furanosyl borate diester; Gases; Homoserine - analogs & derivatives; Homoserine - chemistry; Homoserine - physiology; Lactones - chemistry; LuxP protein; Microbiology; Models, Molecular; Morphology, structure, chemical composition; quorum sensing; Recombinant Fusion Proteins - chemistry; Signal Transduction; Vibrio - chemistry; Vibrio - physiology; Microorganism interrelationships; Cell cell interaction; Autoinducer; Activation; Biological activity; Protein; Characterization; Boron; Vibrio harveyi; Bacteria; Vibrionaceae; Quorum sensing; Structural analysis; Borates; Crystalline structure
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/415545a

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 development. Unlike other autoinducers, which are specific to a particular species of bacteria, a recently discovered autoinducer (AI-2) is produced by a large number of bacterial species. AI-2 has been proposed to serve as a 'universal' signal for inter-species communication. 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.