Proteomic analysis to identify the role of LuxS/AI-2 mediated protein expression in Escherichia coli O157:H7.
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abstract
Microorganisms employ autoinducer molecules to modulate various bacterial processes including virulence expression, biofilm development, and bioluminescence. The universal autoinducer molecule AI-2 is hypothesized to mediate cell signaling in Escherichia coli O157:H7. We investigated the role of AI-2 on the E. coli O157:H7 cellular proteins using a two-dimensional (2D) gel electrophoresis-based proteomic approach. The protein expression patterns between two experimental comparisons were studied namely, 1) a wild type E. coli O157:H7 and its isogenic luxS mutant, and 2) the luxS mutant and the luxS mutant supplemented with AI-2 molecules. Eleven proteins were differentially expressed between the wild type and the luxS mutant strain, whereas 18 proteins were differentially expressed in the luxS mutant strain when supplemented with AI-2. The tryptophan repressor binding protein (WrbA), phosphoglycerate mutase (GpmA), and a putative protein YbbN were found to be differentially expressed under both experimental comparisons. The FliC protein which is involved in flagellar synthesis and motility was up-regulated in the wild type strain but was not influenced by the addition of synthetic AI-2 molecules to the luxS mutant suggesting the involvement of signaling molecules other than AI-2 on flagellar synthesis and motility.
