title: Detection of quorum-sensing-related molecules in Vibrio scophthalmi.
abstract: BACKGROUND
  Cell-to-cell communication (also referred to as quorum sensing) based on N-acyl-homoserine lactones (AHLs) is a widespread response to environmental change in Gram-negative bacteria. AHLs seem to be highly variable, both in terms of the acyl chain length and in the chemical structure of the radicals. Another quorum sensing pathway, the autoinducer-2-based system, is present both in Gram-positive and Gram-negative bacteria. In this study the presence of signal molecules belonging to both quorum sensing signalling pathways was analysed in the marine symbiotic species Vibrio scophthalmi.
  
  
  RESULTS
  Three AHL-like signal molecules were detected in V. scophthalmi supernatants with the Agrobacterium tumefaciens sensor assay. This observation was further supported by the decrease in the presence of these signal molecules after cloning and expression of lactonase AiiA from Bacillus cereus in the V. scophthalmi strains. One of the signal molecules was identified as N-(3-hydroxy dodecanoyl)-L-homoserine lactone. V. scophthalmi was also shown to carry a functional LuxS synthase. The coding sequence for a luxS-like gene was obtained showing a maximum similarity of 78% with Vibrio vulnificus. Analysis of the translated sequence revealed that the sequenced luxS gene carried the conserved domain, which is common to luxS sequences found in other species, and which is essential for LuxS enzymatic activity.
  
  
  CONCLUSIONS
  The data are consistent with the presence of quorum-sensing signal molecules from both AHL- and autoinducer 2-based quorum sensing systems in V. scophthalmi, which are homologous to others previously described in various Vibrio species. How this bacterium interacts with other bacteria and eukaryotic cells to compete ecologically with other intestinal bacteria present in the fish Scophthalmus maximus warrants further investigation.
authors.affiliation: Department of Microbiology, University of Barcelona, Barcelona, Spain. cristina.garcia@cnm.es
authors.forename: Cristina
authors.initials: C
authors.lastname: García-Aljaro
authors.forename: Leo
authors.initials: L
authors.lastname: Eberl
authors.forename: Kathrin
authors.initials: K
authors.lastname: Riedel
authors.forename: Anicet R
authors.initials: AR
authors.lastname: Blanch
mesh_terms: D054742:Acyl-Butyrolactones / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D013437:Carbon-Sulfur Lyases / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D015870:Gene Expression; D008969:Molecular Sequence Data; D010802:Phylogeny; D053038:Quorum Sensing; D016415:Sequence Alignment; D015398:Signal Transduction; D014733:Vibrio / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*
chemical_list: D054742:Acyl-Butyrolactones; D001426:Bacterial Proteins; D013437:Carbon-Sulfur Lyases; C117753:LuxS protein, Bacteria