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Abstract
BackgroundQuorum sensing is a mechanism of cell to cell communication that requires the production and detection of signaling molecules called autoinducers. Although mesophilic bacteria is known to utilize this for synchronization of physiological processes such as bioluminescence, virulence, biofilm formation, motility and cell competency through signaling molecules (acyl homoserine lactones, AI-1; oligopeptides, peptide based system and furanosyl borate diester, AI-2), the phenomenon of quorum sensing in thermophiles is largely unknown.ResultsIn this study, proteomes of 106 thermophilic eubacteria and 21 thermophilic archaea have been investigated for the above three major quorum sensing systems to find the existence of quorum sensing in these thermophiles as there are evidences for the formation of biofilms in hot environments. Our investigation demonstrated that AI-1 system is absent in thermophiles. Further, complete peptide based two component systems for quorum sensing was also not found in any thermophile however the traces for the presence of response regulators for peptide based system were found in some of them. BLASTp search using LuxS (AI-2 synthase) protein sequence of Escherichia coli str. K-12 substr. MG1655 and autoinducer-2 receptors (LuxP of Vibrio harveyi, LsrB of E. coli str. K-12 substr. MG1655 and RbsB of Aggregatibacter actinomycetemcomitans) as queries revealed that 17 thermophilic bacteria from phyla Deinococcus- Thermus and Firmicutes possess complete AI-2 system (LuxS and LsrB and/or RbsB). Out of 106 thermophilic eubacteria 18 from phyla Deinococcus- Thermus, Proteobacteria and Firmicutes have only LuxS that might function as AI-2 synthesizing protein whereas, 16 are having only LsrB and/or RbsB which may function as AI-2 receptor in biofilms.ConclusionsWe anticipate that thermophilic bacteria may use elements of LsrB and RbsB operon for AI-2 signal transduction and they may use quorum sensing for purposes like biofilm formation. Nevertheless, thermophiles in which no known quorum sensing system was found may use some unknown mechanisms as the mode of communication. Further information regarding quorum sensing will be explored to develop strategies to disrupt the biofilms of thermophiles.
Highlights
Quorum sensing is a mechanism of cell to cell communication that requires the production and detection of signaling molecules called autoinducers
Nichols et al [11] demonstrated that two hyperthermophiles, a eubacterium T. maritima, and an archaean Pyrococcus furiosus, produced a response to Vibrio harveyi AI-2 assay despite lacking the autoinducer-2 synthase LuxS
Prevalence of quorum sensing systems in thermophiles The proteomes of 106 thermophilic eubacteria and 21 thermophilic archaea were searched for the presence of autoinducer-1 system through BLASTp using LuxI and LuxR protein sequences of V. fischeri ES114 as query
Summary
Quorum sensing is a mechanism of cell to cell communication that requires the production and detection of signaling molecules called autoinducers. Virulence, bioluminescence, competence, biofilm formation, swarming, sporulation, motility, regulation of stress related genes, optimal growth under iron starvation and antibiotic resistance These processes are controlled by the the three major quorum sensing systems (Autoinducer-1, Peptide based and Autoinducer-2) have been investigated in thermophilic bacteria but still there is limited information on the mechanism of quorum sensing in thermophilic environment [9]. Nichols et al [11] demonstrated that two hyperthermophiles, a eubacterium T. maritima, and an archaean Pyrococcus furiosus, produced a response to Vibrio harveyi AI-2 assay despite lacking the autoinducer-2 synthase LuxS ( known as S-ribosyl homocysteine lyase or S-ribosylhomocysteinase) They further hypothesized that temperature dependent rearrangement of phosphorylated ribose results in formation of AI-2 in these hyperthermophiles. To date, no report exists on the exploration of complete autoinducer-2 pathway comprising autoinducer-2, methylthioadenosine/S-adenosylhomocysteine nucleosidase ( known as MTA/SAH nucleosidase or Pfs) and autoinducer-2 receptor in thermophilic bacteria
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