ArticleVirulence2018
Helicobacter suis binding to carbohydrates on human and porcine gastric mucins and glycolipids occurs via two modes.
Article in Virulence, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 42 citations in OpenAlex.
- Age-related remodeling of the intestinal mucus barrier in pigs: implications for post-weaning diarrhea.Veterinary and animal science · 2026Article
- MUC2 shifts the metabolic profiles of commensal bacteria in defined microbial communities.Microbiome research reports · 2026Article
- Treatment with (R)-α-methylhistamine or IL4 stimulates mucin production and decreasesVirulence · 2025Article
- Hydrogel-based experimental models of the gastrointestinal tract.Microbiome · 2025Review
- Screening and Characterization of Sialic Acid-Binding Variable Lymphocyte Receptors from Hagfish.Biotech (Basel (Switzerland)) · 2024Article
- Characterization of the rainbow trout (Oncorhynchus mykiss) mucosal glycosphingolipid repertoire and Aeromonas salmonicida binding to neutral glycosphingolipids.Glycobiology · 2024Article
- The prevalence of porcine gastric ulcer and Helicobacter suis in Taiwan.The Journal of veterinary medical science · 2024Article
- Mucus polymer concentration andmBio · 2024Article
- Labeling of Mucin-TypeACS measurement science au · 2024Article
- How Does Airway Surface Liquid Composition Vary in Different Pulmonary Diseases, and How Can We Use This Knowledge to Model Microbial Infections?Microorganisms · 2024Review
- Exploring the Differential Expression of a Set of Key Genes Involved in the Regulation and Functioning of the Stomach in the Post-Weaned Pig.Veterinary sciences · 2023Article
- Immunohistochemical detection of MUC5AC and MUC5B mucins in ferrets.BMC research notes · 2023Article
- O-Mucin-degrading carbohydrate-active enzymes and their possible implication in inflammatory bowel diseases.Essays in biochemistry · 2023Review
- Article
- Role of mucus-bacteria interactions in Enterotoxigenic Escherichia coli (ETEC) H10407 virulence and interplay with human microbiome.NPJ biofilms and microbiomes · 2022Article
- Gastric Helicobacter species associated with dogs, cats and pigs: significance for public and animal health.Veterinary research · 2022Review
- Article
- Host-pathogen protein-nucleic acid interactions: A comprehensive review.Computational and structural biotechnology journal · 2022Review
- Article
- Impact of the Epithelial Lining Fluid Milieu on Amikacin Pharmacodynamics Against Pseudomonas aeruginosa.Drugs in R&D · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Helicobacter suis colonizes the stomach of most pigs and is the most prevalent non-Helicobacter pylori Helicobacter species found in the human stomach. In the human host, H. suis contributes to the development of chronic gastritis, peptic ulcer disease and MALT lymphoma, whereas in pigs it is associated with gastritis, decreased growth and ulcers. Here, we demonstrate that the level of H. pylori and H. suis binding to human and pig gastric mucins varies between individuals with species dependent specificity. The binding optimum of H. pylori is at neutral pH whereas that of H. suis has an acidic pH optimum, and the mucins that H. pylori bind to are different than those that H. suis bind to. Mass spectrometric analysis of mucin O-glycans from the porcine mucin showed that individual variation in binding is reflected by a difference in glycosylation; of 109 oligosaccharide structures identified, only 14 were present in all examined samples. H. suis binding to mucins correlated with glycans containing sulfate, sialic acid and terminal galactose. Among the glycolipids present in pig stomach, binding to lactotetraosylceramide (Galβ3GlcNAcβ3Galβ4Glcβ1Cer) was identified, and adhesion to Galβ3GlcNAcβ3Galβ4Glc at both acidic and neutral pH was confirmed using other glycoconjugates. Together with that H. suis bound to DNA (used as a proxy for acidic charge), we conclude that H. suis has two binding modes: one to glycans terminating with Galβ3GlcNAc, and one to negatively charged structures. Identification of the glycan structures H. suis interacts with can contribute to development of therapeutic strategies alternative to antibiotics.
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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.