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dc.contributor.authorReuter, Mark
dc.contributor.authorPeriago, Paula
dc.contributor.authorMulholland, Francis
dc.contributor.authorBrown, Helen Louise
dc.contributor.authorVan Vliet, Arnoud
dc.date.accessioned2019-11-05T12:21:46Z
dc.date.available2019-11-05T12:21:46Z
dc.date.issued2015-07-30
dc.identifier.citationReuter, M., Periago, P.M., Mulholland, F., Brown, H.L. and Van Vliet, A.H. (2015) 'A PAS domain-containing regulator controls flagella-flagella interactions in Campylobacter jejuni', Frontiers in Microbiology, 6, p.770. DOI: 10.3389/fmicb.2015.00770.en_US
dc.identifier.issn1664-302X
dc.identifier.urihttp://hdl.handle.net/10369/10825
dc.descriptionArticle published in Frontiers in Microbiology on 30 July 2015, available open access at: https://doi.org/10.3389/fmicb.2015.00770.en_US
dc.description.abstractThe 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 Δcj1387c 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 Δcj1388 and Δcj0327 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.en_US
dc.description.sponsorshipBiotechnology and Biological Sciences Research Council (BBSRC) via the BBSRC Institute Strategic Programme (BB/J004529/1). Paula M. Periago thanks the Spanish Ministerio de Ciencia e Innovación for the grant of the Programa Nacional de Movilidad de Recursos Humanos del Plan Nacional de I-D+i 2008–2011. Helen Brown was funded from BBSRC CASE studentship (BB/I15321/1) with CASE funding from Campden BRI.en_US
dc.language.isoenen_US
dc.publisherFrontiers Mediaen_US
dc.relation.ispartofseriesFrontiers in Microbiology;
dc.titleA PAS domain-containing regulator controls flagella-flagella interactions in Campylobacter jejunien_US
dc.typeArticleen_US
dc.identifier.doihttps://doi.org/10.3389/fmicb.2015.00770
dcterms.dateAccepted2015-07-14
rioxxterms.funderCardiff Metropolitan Universityen_US
rioxxterms.identifier.projectCardiff Metropolian (Internal)en_US
rioxxterms.versionVoRen_US
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/en_US
rioxxterms.licenseref.startdate2019-11-05
rioxxterms.funder.project37baf166-7129-4cd4-b6a1-507454d1372een_US


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