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that they have no competing interests. Authors’ contributions W-JS and F-JC conceived of the study, participated in its design and coordination, and drafted the manuscript. C-FL performed experiments and analyzed results and helped to draft the manuscript. YL, S-LY and LS performed partial experiments and analyzed results. All authors read and approved the manuscript.”
“Background Campylobacter jejuni is a causative agent of acute bacterial gastroenteritis in humans, and is responsible for an estimated 500 million cases XAV-939 mouse annually worldwide [1, 2]. Although this bacterium poses a significant Evodiamine economic burden, little is known or understood about
the mechanisms of pathogenicity. Some factors, however, have been ascertained to contribute LY2835219 toward the overall pathogenicity of the infecting strain such as chemotaxis, adherence to host cells and surface glycans including lipooligosaccharide [3]. Chemotaxis and motility have been implicated in the colonisation and virulence of many pathogenic bacteria such as Escherichia coli, Salmonella enterica serovar Typhimurium, as well as C. jejuni[3, 4]. Homologues of the chemotactic pathway have been identified in C. jejuni NCTC 11168 and include ten putative chemotactic sensory receptors, Tlps, and two aerotaxis receptors [5]. The receptors are grouped according to their putative function as assigned by homology to known chemoreceptors of other organisms [5, 6]. The group A consist of Tlp1, 2, 3, 4, 7 and 10, all of which contain distinct domains comprising of two transmembrane domains, a sensory domain and a highly conserved cytoplasmic domain [5]. Due to similarity to methyl-accepting chemotactic proteins from other bacterial species, group A Tlp receptors are thought likely to sense ligands external to the cell [5]. Only two of the group A Tlp proteins of C. jejuni have been characterised to date, the aspartate receptor, Tlp1 [7] and Tlp7 which binds to formic acid [8].