High-affinity binding of Clostridium perfringens epsilon-toxin to rat brain.
125I-epsilon-toxin showed high affinity to rat brain homogenates and synaptosomal membrane fractions, having single binding phases with dissociation constants (Kds) of 2.5 and 3.3 nM, respectively. Treatment of synaptosomal membrane fractions with pronase and neuraminidase lowered the binding of the labeled toxin, whereas treatment with trypsin and phospholipase C did not. Heating of the fractions resulted in a decrease in the binding of the toxin. These data suggest that interaction of epsilon-toxin with cell membranes in the brain is facilitated by a sialoglycoprotein. On the other hand, treatment of the membrane fractions with lipase resulted in complete loss of binding, suggesting that the interaction may require an appropriate lipid environment. These data suggest the presence of specific binding sites in brain tissue for epsilon-toxin.
Nagahama
M
M
Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Japan.
Sakurai
J
J
D000818:Animals; D001427:Bacterial Toxins / Q000378:metabolism* / Q000633:toxicity; D001665:Binding Sites; D001921:Brain / Q000378:metabolism*; D002038:Bungarotoxins / Q000494:pharmacology; D003016:Clostridium perfringens / Q000472:pathogenicity*; D066298:In Vitro Techniques; D051381:Rats; D012795:Sialoglycoproteins / Q000378:metabolism; D013574:Synaptosomes / Q000378:metabolism
D001427:Bacterial Toxins; D002038:Bungarotoxins; C039811:Clostridium perfringens epsilon-toxin; D012795:Sialoglycoproteins