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Campylobacter 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(β1–3)-GalNAc(β1–4)-GalNAc(β1–4)-GalNAcα1-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.

open biology

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

A novelO-linked glycan modulatesCampylobacter jejunimajor outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization