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

Mahdavi, Jafar; Pirinccioglu, Necmettin; Oldfield, Neil J.; Carlsohn, Elisabet; Stoof, Jeroen; Aslam, Akhmed; Self, Tim; Cawthraw, Shaun A.; Petrovska, Liljana; Colborne, Natalie; Sihlbom, Carina; Boren, Thomas; Wooldridge, Karl G.; Ala'Aldeen, Dlawer A.A.

Authors

Jafar Mahdavi

Necmettin Pirinccioglu

Neil J. Oldfield

Elisabet Carlsohn

Jeroen Stoof

Akhmed Aslam

Tim Self

Shaun A. Cawthraw

Liljana Petrovska

Natalie Colborne

Carina Sihlbom

Thomas Boren

Karl G. Wooldridge

Dlawer A.A. Ala'Aldeen



Abstract

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 Thr268; previously only flagellin proteins were known to be O-glycosylated in C. jejuni. Substitution of MOMP Thr268 led to significantly reduced binding to BgAgs. The O-glycan moiety was characterized as Gal(β1–3)-GalNAc(β1–4)-GalNAc(β1–4)-GalNAcα1-Thr268; modelling suggested that O-glycosylation has a notable effect on the conformation of MOMP and this modulates BgAg-binding capacity. Glycosylation of MOMP at Thr268 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.

Journal Article Type Article
Publication Date Jan 22, 2014
Journal Open Biology
Electronic ISSN 2046-2441
Publisher Royal Society, The
Peer Reviewed Peer Reviewed
Volume 4
Issue 1
Article Number 130202
Institution Citation Mahdavi, J., Pirinccioglu, N., Oldfield, N. J., Carlsohn, E., Stoof, J., Aslam, A., …Ala'Aldeen, D. A. (2014). A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization. Open Biology, 4(1), doi:10.1098/rsob.130202
DOI https://doi.org/10.1098/rsob.130202
Keywords Campylobacter jejuni, histo-blood group antigens, FlaA, major outer membrane protein, O-glycosylation, biofilm
Publisher URL http://rsob.royalsocietypublishing.org/content/4/1/130202
Copyright Statement Copyright information regarding this work can be found at the following address: http://creativecommons.org/licenses/by/4.0

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Copyright Statement
Copyright information regarding this work can be found at the following address: http://creativecommons.org/licenses/by/4.0





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