A loss of LuxS function impacts on motility-associated genes in a range of different bacteria. For enterohemorrhagicE. coli(EHEC),H. pylori, andC. jejunia role of AI-2 in the regulation of motility associated genes has been proposed [35,44,60,61]. At least forC. jejuni, this view is not supported by the data contained

within the present study. The defect in motility caused by deletion ofluxSinH. pyloriwas shown to be restored by addition of cell free medium containing AI-2 [62], but this could not be demonstrated for theC. jejuni luxSmutant in this study. The flagella regulatorflhAwas also shown to be induced by addition of AI-2 in aluxSmutant background Selleck LXH254 providing further evidence for the role of AI-2 in the global regulation of flagella gene transcription [62]. In contrast, transcription offlhAwas not altered in aluxSmutant ofC. jejuni(this study and [37]). A phylogenetic tree of the LuxS protein revealed that the LuxS ofC. jejuniis phylogenetically distant to that ofH. pyloriwhich could, in part, explain differences in function between the LuxS protein inC. jejuniandH. pylori[63]. Since it was probably acquired independently in the two species, the primary role taken on byluxS(gene regulation versus metabolic) would differ depending on what other pathways were already established. AI-2 production and degradation Virtually no AI-2 activity was detectable whenC. jejuniNCTC 11168 was grown in

MEM-α. This could be due to a lack of AI-2 export, G418 order rapid intracellular turnover of DPD or AI-2 or lack ofluxSorpfsexpression and thus DPD synthesis. The latter possibility could not be ruled out, as it was not possible to detect Pfs and LuxS enzyme activity

in cell extracts obtained from strain NCTC 11168 growing in MEM-α or in MHB. The reason for PDK4 this remains unclear, as SAH and SRH conversion could be detected in similarly preparedE. colicell extracts. It could be that inC. jejuni, enzyme activity levels are below those detectable in the assay. There is unCapmatinib supplier likely to be an absence ofpfsexpression in MEM-α, as previous studies have indicated modulatedpfsexpression [58] rather than an on/off control. Moreover,pfsmutations cause severe growth defects [64]. Given the absence of a growth defect in MEM-α, Pfs is likely to be present. In support of this, although the differential expression was not significant (confidence level was 18%, based on two separate P-values; slope and intercept), theluxSmutant had 1.9 fold morepfsexpression than the WT in MEM-α. The overall differential gene expression detected in MEM-α suggests that the WT, but not the mutant produces LuxS. Exogenous AI-2 activity gradually diminished when added to MHB or MEM-α grownC. jejunicultures suggesting either uptake or degradation. However,C. jejunidoes not seem to possess an AI-2 uptake system homologous to that found inS. Typhimurium andE. coli.