Cardiff University | Prifysgol Caerdydd ORCA
Online Research @ Cardiff 
WelshClear Cookie - decide language by browser settings

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

Reuter, Mark, Periago, Paula M., Mulholland, Francis, Brown, Helen L. and van Vliet, Arnoud H. M. 2015. A PAS domain-containing regulator controls flagella-flagella interactions in Campylobacter jejuni. Frontiers in Microbiology 6 , 770. 10.3389/fmicb.2015.00770

[thumbnail of Reuter-2015-A-pas-domain-containing-regulator-c.pdf] PDF - Published Version
Available under License Creative Commons Attribution Non-commercial No Derivatives.

Download (2MB)

Abstract

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 1cj1387c 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 1cj1388 and 1cj0327 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. Keywords: Campylobacter, flagella, transcriptional repression, PAS domains.

Item Type: Article
Date Type: Published Online
Status: Published
Schools: Dentistry
Publisher: Frontiers Media
ISSN: 1664-302X
Funders: BBSRC
Date of First Compliant Deposit: 7 September 2020
Date of Acceptance: 14 July 2015
Last Modified: 05 May 2023 08:59
URI: https://orca.cardiff.ac.uk/id/eprint/134669

Citation Data

Cited 10 times in Scopus. View in Scopus. Powered By Scopus® Data

Actions (repository staff only)

Edit Item Edit Item

Downloads

Downloads per month over past year

View more statistics