Helicobacter pylori and Neutrophils: Sialic Acid-Dependent Binding to Various Isolated Glycoconjugates
| Autor: | Halina Miller-Podraza, Karl-Anders Karlsson, Jörgen Bergström, Maan Abul Milh, Marianne Longard, Britt-Marie Olsson, Susann Teneberg, Lotta Uggla |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Neutrophils
Glycoconjugate Immunology Biology Microbiology chemistry.chemical_compound Glycolipid Gangliosides Humans Glycoproteins chemistry.chemical_classification Ganglioside Helicobacter pylori biology.organism_classification N-Acetylneuraminic Acid Sialic acid Infectious Diseases chemistry Biochemistry Molecular and Cellular Pathogenesis biology.protein Electrophoresis Polyacrylamide Gel Parasitology Chromatography Thin Layer Glycoprotein Glycoconjugates N-Acetylneuraminic acid Neuraminidase Bacteria |
| Zdroj: | Infection and Immunity. 67:6309-6313 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.67.12.6309-6313.1999 |
| Popis: | Helicobacter pylori has been shown to agglutinate erythrocytes in a sialic acid-dependent manner. However, very few studies have examined relevant target cells in the human stomach. Neutrophils are required for the onset of gastritis, and the inflammatory reaction may be induced on contact between bacteria and neutrophils. In the present work, glycolipids and glycoproteins were isolated from neutrophils and were studied for binding by overlay with radiolabeled bacteria on thin-layer chromatograms and on membrane blots. There was a complex pattern of binding bands. The only practical binding activity found was sialic acid dependent, since treatment of glycoconjugates with neuraminidase or mild periodate eliminated binding. As shown before for binding to erythrocytes and other glycoconjugates, bacterial cells grown on agar bound to many glycoconjugates, while growth in broth resulted in bacteria that would bind only to polyglycosylceramides, which are highly heterogeneous and branched poly- N -acetyllactosamine-containing glycolipids. Approximately seven positive bands were found for glycoproteins, and the traditional ganglioside fraction showed a complex, slow-moving interval with very strong sialic-acid-dependent binding, probably explained by Fuc substitutions on GlcNAc. |
| Databáze: | OpenAIRE |
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