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

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