Glycosphingolipid Recognition by F4 Fimbriae of Enterotoxigenic Escherichia coli
Author Information
Author(s): Coddens Annelies, Valis Erik, Benktander John, Ångström Jonas, Breimer Michael E., Cox Eric, Teneberg Susann
Primary Institution: Laboratory of Veterinary Immunology, Faculty of Veterinary Medicine, Ghent University, Belgium
Hypothesis
The study investigates the binding of F4 fimbriae variants to glycosphingolipids from porcine intestinal epithelium and erythrocytes.
Conclusion
The F4 fimbriae variants exhibit distinct binding patterns to specific glycosphingolipids, which may influence their role in E. coli adhesion and pathogenesis in pigs.
Supporting Evidence
- F4 fimbriae variants bind to different glycosphingolipids, indicating specificity in adhesion.
- Two novel glycosphingolipids were identified from chicken erythrocytes.
- F4ab and F4ac fimbriae showed selective binding patterns to specific glycosphingolipids in porcine intestinal epithelium.
Takeaway
This study looks at how certain bacteria stick to pig intestines by grabbing onto special sugars found in the cells, which helps them cause diarrhea.
Methodology
The binding of isolated F4 fimbriae and F4-fimbriated E. coli to glycosphingolipids from various sources was examined using mass spectrometry and NMR.
Limitations
The study primarily focuses on specific glycosphingolipids and may not encompass all potential binding interactions.
Digital Object Identifier (DOI)
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