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Biochemistry |
Department of Bacteriology, Okayama University Medical School, 2-5-1 Shikata-cho, Okayama 700-8558, Japan1
Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan2
Department of Food Science, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri099-2422, Japan3
Author for correspondence: Keiji Oguma. Tel: +81 86 235 7162. Fax: +81 86 235 7162. e-mail: kuma{at}med.okayama-u.ac.jp
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-
-N-acetylgalactosaminidase treatment did not. Thus these results can be interpreted as indicating that type A HA+-PTX detects and binds to Galß1-4GlcNAc 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.
Keywords: binding, sugar chain, glycolipid, glycoprotein
Abbreviations: CBB, Coomassie brilliant blue; HA, haemagglutinin; HA+-PTX, haemagglutinin-positive progenitor toxin; PAS, periodic acid–Schiff
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