Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA(+)-PTX) binds to oligosaccharides containing Gal beta 1-4GlcNAc through onesubcomponent of haemagglutinin (HA1)

Citation
K. Inoue et al., Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA(+)-PTX) binds to oligosaccharides containing Gal beta 1-4GlcNAc through onesubcomponent of haemagglutinin (HA1), MICROBIO-UK, 147, 2001, pp. 811-819
Citations number
27
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
MICROBIOLOGY-UK
ISSN journal
1350-0872 → ACNP
Volume
147
Year of publication
2001
Part
4
Pages
811 - 819
Database
ISI
SICI code
1350-0872(200104)147:<811:CBTAHP>2.0.ZU;2-N
Abstract
Haemagglutinin (HA) activity of Clostridium botulinum type A 19S and 16S to xins (HA-positive progenitor toxin; HA(+)-PTX) was characterized. HA titres against human erythrocytes of HA(+)-PTX were inhibited by the addition of lactose, D-gatactose, 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 n ot bind to gangliosides. Type A HA(+)-PTX also bound to asialoglycoproteins (asialofetuin, neuraminidase-treated transferrin). but not to sialoglycopr oteins (fetuin, transferrin). Although glycopeptidase F treatment of asialo fetuin abolished the binding of HA(+)-PTX, endo-alpha -N-acetylgalactosamin idase treatment did not. Thus these results can be interpreted as indicatin g that type A HA(+)-PTX detects and kinds to Gal beta1-4GlcNAc in paraglobo side and the N-linked oligosaccharides of glycoproteins. Regardless of neur aminidase treatment type A HA(+)-PTX bound to glycophorin A which is a majo r sialoglycoprotein on the surface of erythrocytes. Both native glycophorin A and neuraminidase-treated glycophorin A inhibited the binding of erythro cytes to type A HA(+)-PTX. Since the N-linked oligosaccharide of glycophori n 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 subcom ponent of HA, designated HA1, did not agglutinate native erythrocytes, alth ough it did bind to erythrocytes, paragloboside and asialoglycoproteins in a manner quite similar to that of HA(+)-PTX. These results indicate that ty pe A HA(+)-PTX binds to oligosaccharides through HA1.