A PAS domain-containing regulator controls flagella-flagella interactions in Campylobacter jejuni

作者: Mark Reuter , Paula M. Periago , Francis Mulholland , Helen L. Brown , Arnoud H. M. van Vliet

DOI: 10.3389/FMICB.2015.00770

关键词:

摘要: The bipolar flagella of the foodborne bacterial pathogen Campylobacter jejuni confer motility, which is essential for virulence. C. are post-translationally modified, but how this process controlled not well understood. In work, we have identified a novel PAS-domain containing regulatory system, modulates flagella-flagella interactions in jejuni. Inactivation cj1387c gene, encoding YheO-like PAS6 domain linked to helix-turn-helix domain, resulted generation tightly associated "cell-train" morphotype, where up four cells were connected by their flagella. morphotype was fully motile, resistant vortexing, accompanied increased autoagglutination, and observed aflagellated cells. Δcj1387c mutant displayed expression adjacent Cj1388 protein, comprises single endoribonuclease L-PSP domain. Comparative genomics showed that (yheO) orthologs genomes commonly an cj1388 ortholog, with some bacteria, including jejuni, another cj1388-like gene (cj0327). cj0327 genes decreased autoagglutination Tween-20-supplemented media. Δcj1388 Δcj0327 mutants also attenuated Galleria larvae-based infection model. Finally, substituting sole cysteine serine prevented dimerization non-reducing conditions, presence Tween-20. We hypothesize Cj0327 modulate post-translational modification through yet unidentified mechanisms, propose naming Cj1387 Flagella Interaction Regulator CfiR, protein as CfiP CfiQ, respectively.

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