ArticleOpen biology2014
A novel O-linked glycan modulates Campylobacter jejuni major outer membrane protein-mediated adhesion to human histo-blood group antigens and chicken colonization.
Article in Open biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 63 citations in OpenAlex.
- Uncovering bacterial pseudaminylation with pan-specific antibody tools.Nature chemical biology · 2026Article
- Bacterial post-translational changes: the possible enigma of multidrug resistance.Archives of microbiology · 2026Review
- How flagellar glycosylation of the phytopathogenic bacteriumApplied and environmental microbiology · 2026Article
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Native gastrointestinal mucus: Critical features and techniques for studying interactions with drugs, drug carriers, and bacteria.Advanced drug delivery reviews · 2023Review
- Ferric quinate (QPLEX) inhibits the interaction of major outer membrane protein (MOMP) with the Lewis b (LeFrontiers in microbiology · 2023Article
- Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) ofComputational and structural biotechnology journal · 2022Article
- Mucin-Type O-Glycans: Barrier, Microbiota, and Immune Anchors in Inflammatory Bowel Disease.Journal of inflammation research · 2021Review
- Intestinal inflammation alters mucosal carbohydrate foraging and monosaccharide incorporation into microbial glycans.Cellular microbiology · 2021Article
- Bridging the Gap: A Role forMicroorganisms · 2020Review
- The Rho-Independent Transcription Terminator for theInfection and immunity · 2019Article
- Comparative analysis of amplicon and metagenomic sequencing methods reveals key features in the evolution of animal metaorganisms.Microbiome · 2019Article
- Proteome Profiling by Label-Free Mass Spectrometry Reveals Differentiated Response of Campylobacter jejuni 81-176 to Sublethal Concentrations of Bile Acids.Proteomics. Clinical applications · 2019Article
- The Prevalence of Virulence Genes and Multidrug Resistance in ThermophilicOpen life sciences · 2019Article
- Functional analysis of the Helicobacter pullorum N-linked protein glycosylation system.Glycobiology · 2018Article
- TYPLEX® Chelate, a novel feed additive, inhibits Campylobacter jejuni biofilm formation and cecal colonization in broiler chickens.Poultry science · 2018Article
- Nanobodies targeting conserved epitopes on the major outer membrane protein of Campylobacter as potential tools for control of Campylobacter colonization.Veterinary research · 2017Article
- Transcriptome and proteome dynamics in chemostat culture reveal how Campylobacter jejuni modulates metabolism, stress responses and virulence factors upon changes in oxygen availability.Environmental microbiology · 2017Article
- Mechanisms and consequences of intestinal dysbiosis.Cellular and molecular life sciences : CMLS · 2017Review
- The Periplasmic Chaperone Network ofFrontiers in microbiology · 2017Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
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 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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.