The AHL- and BDSF-dependent quorum sensing systems control specific and overlapping sets of genes in Burkholderia cenocepacia H111

• Published in: PloS one Vol. 7; no. 11; p. e49966
• Main Authors: Schmid, Nadine, Pessi, Gabriella, Deng, Yinyue, Aguilar, Claudio, Carlier, Aurelien L, Grunau, Alexander, Omasits, Ulrich, Zhang, Lian-Hui, Ahrens, Christian H, Eberl, Leo
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 20.11.2012; Public Library of Science (PLoS)
• Subjects: Acyl-Butyrolactones - metabolism; Analysis; Bacteria; Bacterial genetics; Biofilms; Biology; Bradyrhizobium japonicum; Burkholderia cenocepacia; Burkholderia cenocepacia - genetics; Burkholderia cenocepacia - metabolism; Burkholderia cenocepacia - pathogenicity; Burkholderia cepacia; Cell Communication - genetics; Chromosomes; Control systems; Cystic fibrosis; Fatty Acids, Monounsaturated - metabolism; Gene expression; Gene Expression Regulation, Bacterial; Genes; Genes, Bacterial; Genomes; Genomics; Glycine max; Homoserine lactones; Lactones; Lectins; Life sciences; Machinery and equipment; Motility; Operons; Pathogenicity; Pathogens; Peptide Hydrolases - biosynthesis; Peptide Hydrolases - genetics; Proteases; Proteins; Proteolysis; Proteomics; Quorum Sensing - genetics; Ribonucleic acid; RNA; RNA sequencing; Secretion; Signal Transduction - genetics; Signalling systems; Studies; Singapore
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0049966

Quorum sensing in Burkholderia cenocepacia H111 involves two signalling systems that depend on different signal molecules, namely N-acyl homoserine lactones (AHLs) and the diffusible signal factor cis-2-dodecenoic acid (BDSF). Previous studies have shown that AHLs and BDSF control similar phenotypic traits, including biofilm formation, proteolytic activity and pathogenicity. In this study we mapped the BDSF stimulon by RNA-Seq and shotgun proteomics analysis. We demonstrate that a set of the identified BDSF-regulated genes or proteins are also controlled by AHLs, suggesting that the two regulons partially overlap. The detailed analysis of two mutually regulated operons, one encoding three lectins and the other one encoding the large surface protein BapA and its type I secretion machinery, revealed that both AHLs and BDSF are required for full expression, suggesting that the two signalling systems operate in parallel. In accordance with this, we show that both AHLs and BDSF are required for biofilm formation and protease production.