title: Binding of bacterial toxins to glycoproteins in the envelopes of rainbow trout eggs.
abstract: The ability of the vitelline and fertilization envelopes of rainbow trout eggs to trap toxins was investigated using cholera enterotoxin B and staphylococcal enterotoxin B in cytochemical or immunocytochemical experiments. Extracts from both envelopes were investigated by immunoblot analysis to identify toxin-binding proteins after SDS-PAGE. Binding studies of cholera enterotoxin B to vitelline envelopes and fertilization envelopes revealed a greater reactive intensity in the former. Treatment with neuraminidase enhanced the reactive intensity (or deposit) in the vitelline envelope and fertilization envelope outermost layers, with more conspicuous reactivity in the former. Cytochemical experiments showed that exogenous ganglioside GM1 considerably enhanced cholera enterotoxin B binding to vitelline and fertilization envelopes. This enhancement was shown by an intense reactivity following the occurrence of new binding sites on the vitelline envelope inner surface and the inner wall of the zona radiata, a simultaneous extreme reduction in the reactivity of the vitelline envelope outermost layer, and a striking increase in reactive products in the fertilization envelope outermost layer. The surface region of the vitelline or fertilization envelope outermost layer was the binding site for staphylococcal enterotoxin B, and neuraminidase treatment caused a considerable reduction of reactive products in these areas. Immunoblot analysis of cholera enterotoxin B- or staphylococcal enterotoxin B-binding substances in extracts from the vitelline envelopes or fertilization envelopes demonstrated that the great majority of the binding substances are glycoproteins. The present results suggest that glycoproteins constituting the vitelline envelope or fertilization envelope may contribute to the protection of the egg itself or the embryo by trapping noxious toxins.
authors.affiliation: Department of Anatomy, Gunma University School of Medicine, Maebashi, Japan.
authors.forename: S
authors.initials: S
authors.lastname: Kudo
authors.forename: S
authors.initials: S
authors.lastname: Yazawa
mesh_terms: D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism*; D002772:Cholera Toxin / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004768:Enterotoxins / Q000378:metabolism; D005677:G(M1) Ganglioside / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism; D015151:Immunoblotting; D007150:Immunohistochemistry; D017686:Oncorhynchus mykiss / Q000378:metabolism*; D010063:Ovum / Q000378:metabolism*; D013210:Staphylococcus / Q000378:metabolism; D014817:Vitelline Membrane / Q000378:metabolism
chemical_list: D001427:Bacterial Toxins; D004768:Enterotoxins; D006023:Glycoproteins; D005677:G(M1) Ganglioside; C031818:enterotoxin B, staphylococcal; D002772:Cholera Toxin; D006735:Horseradish Peroxidase