Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA+-PTX) binds to oligosaccharides containing Galβ1-4GlcNAc through one subcomponent of haemagglutinin (HA1)
| Autor: | Nazira Mahmut, Keiji Oguma, Koichi Honke, Hideyuki Arimitsu, Katsuhiro Inoue, Yoshihiko Sakaguchi, Kaoru Inoue, Toshihiro Watanabe, Yukako Fujinaga, Tohru Ohyama |
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| Rok vydání: | 2001 |
| Předmět: |
Acetylgalactosamine
Immunoblotting Oligosaccharides complex mixtures Microbiology Glycolipid Asialoglycoproteins Sialoglycoprotein Lectins Clostridium botulinum Humans Glycophorin Botulinum Toxins Type A Glycoproteins chemistry.chemical_classification Chromatography Globosides biology Glycolipid binding Hemagglutination Tests Hemagglutination Inhibition Tests Hemagglutinin Oligosaccharide Fetuin Hemagglutinins Biochemistry chemistry biology.protein Electrophoresis Polyacrylamide Gel Glycolipids Protein Binding |
| Zdroj: | Microbiology. 147:811-819 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/00221287-147-4-811 |
| Popis: | Haemagglutinin (HA) activity of Clostridium botulinum type A 19S and 16S toxins (HA-positive progenitor toxin; HA(+)-PTX) was characterized. HA titres against human erythrocytes of HA(+)-PTX were inhibited by the addition of lactose, D-galactose, N-acetyl-D-galactosamine and D-fucose to the reaction mixtures. A direct glycolipid binding test demonstrated that type A HA(+)-PTX strongly bound to paragloboside and some neutral glycolipids, but did not bind to gangliosides. Type A HA(+)-PTX also bound to asialoglycoproteins (asialofetuin, neuraminidase-treated transferrin), but not to sialoglycoproteins (fetuin, transferrin). Although glycopeptidase F treatment of asialofetuin abolished the binding of HA(+)-PTX, endo-alpha-N-acetylgalactosaminidase treatment did not. Thus these results can be interpreted as indicating that type A HA(+)-PTX detects and binds to Gal beta 1-4GlcNAc in paragloboside and the N-linked oligosaccharides of glycoproteins. Regardless of neuraminidase treatment, type A HA(+)-PTX bound to glycophorin A which is a major sialoglycoprotein on the surface of erythrocytes. Both native glycophorin A and neuraminidase-treated glycophorin A inhibited the binding of erythrocytes to type A HA(+)-PTX. Since the N:-linked oligosaccharide of glycophorin A is di-branched and more than 50% of this sugar chain is monosialylated, type A HA(+)-PTX probably bound to the unsialylated branch of the N-linked oligosaccharide of glycophorin A and agglutinated erythrocytes. One subcomponent of HA, designated HA1, did not agglutinate native erythrocytes, although it did bind to erythrocytes, paragloboside and asialoglycoproteins in a manner quite similar to that of HA(+)-PTX. These results indicate that type A HA(+)-PTX binds to oligosaccharides through HA1. |
| Databáze: | OpenAIRE |
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