A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization

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dc.contributor.authorMahdavi, Jafar
dc.contributor.authorPirinccioglu, Necmettin
dc.contributor.authorOldfield, Neil J.
dc.contributor.authorCarlsohn, Elisabet
dc.contributor.authorStoof, Jeroen
dc.contributor.authorAslam, Akhmed
dc.contributor.authorSelf, Tim
dc.date.accessioned2024-04-24T17:08:37Z
dc.date.available2024-04-24T17:08:37Z
dc.date.issued2014
dc.departmentDicle Üniversitesien_US
dc.description.abstractCampylobacter jejuni is an important cause of human foodborne gastroenteritis; strategies to prevent infection are hampered by a poor understanding of the complex interactions between host and pathogen. Previous work showed that C. jejuni could bind human histo-blood group antigens (BgAgs) in vitro and that BgAgs could inhibit the binding of C. jejuni to human intestinal mucosa ex vivo. Here, the major flagella subunit protein (FlaA) and the major outer membrane protein (MOMP) were identified as BgAg-binding adhesins in C. jejuni NCTC11168. Significantly, the MOMP was shown to be O-glycosylated at Thr(268); previously only flagellin proteins were known to be O-glycosylated in C. jejuni. Substitution of MOMP Thr(268) led to significantly reduced binding to BgAgs. The O-glycan moiety was characterized as Gal(beta 1-3)-GalNAc(beta 1-4)-GalNAc(beta 1-4)-GalNAca1-Thr(268); modelling suggested that O-glycosylation has a notable effect on the conformation of MOMP and this modulates BgAg-binding capacity. Glycosylation of MOMP at Thr(268) promoted cell-to-cell binding, biofilm formation and adhesion to Caco-2 cells, and was required for the optimal colonization of chickens by C. jejuni, confirming the significance of this O-glycosylation in pathogenesis.en_US
dc.description.sponsorshipMedical Research Council (MRC), UK [G0901696]; Medical Research Council [G0901696] Funding Source: researchfish; MRC [G0901696] Funding Source: UKRIen_US
dc.description.sponsorshipThis work was supported by the Medical Research Council (MRC), UK (grant no. G0901696).en_US
dc.identifier.doi10.1098/rsob.130202
dc.identifier.issn2046-2441
dc.identifier.issue1en_US
dc.identifier.pmid24451549
dc.identifier.scopus2-s2.0-84901049521
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.1098/rsob.130202
dc.identifier.urihttps://hdl.handle.net/11468/17400
dc.identifier.volume4en_US
dc.identifier.wosWOS:000332387600003
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoenen_US
dc.publisherRoyal Socen_US
dc.relation.ispartofOpen Biology
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCampylobacter Jejunien_US
dc.subjectHisto-Blood Group Antigensen_US
dc.subjectFlaaen_US
dc.subjectMajor Outer Membrane Proteinen_US
dc.subjectO-Glycosylationen_US
dc.subjectBiofilmen_US
dc.titleA novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonizationen_US
dc.titleA novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization
dc.typeArticleen_US

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