TLC immunostaining characterization of Clostridium botulinum type A neurotoxin binding to gangliosides and free fatty acids.
The receptor structure of Clostridium botulinum neurotoxin type A was analysed by TLC immunostaining. GQ1b was found to be the most potent receptor, and the neurotoxin also bound to GT1b and GD1a, but not to GM3, GM2, GM1, GD3, GD1b and GT1a. Optimum binding of neurotoxin to the ganglioside appeared in 0.01 M phosphate buffer (pH 7.2) containing 0.2% NaCl. Higher and lower NaCl concentrations diminished neurotoxin binding to the ganglioside. In addition, the neurotoxin was able to bind to free fatty acids. Maximum binding was observed on stearic acid and neurotoxin binding to free fatty acids was not affected by NaCl concentration.
Takamizawa
K
K
Iwamori
M
M
Kozaki
S
S
Sakaguchi
G
G
Tanaka
R
R
Takayama
H
H
Nagai
Y
Y
D001905:Botulinum Toxins / Q000378:metabolism*; D005230:Fatty Acids, Nonesterified / Q000378:metabolism*; D005732:Gangliosides / Q000378:metabolism*; D006801:Humans; D050356:Lipid Metabolism; D008895:Milk, Human / Q000032:analysis
D005230:Fatty Acids, Nonesterified; D005732:Gangliosides; C021298:ganglioside, GD1a; C016481:trisialoganglioside GT1; C039129:GQ1b ganglioside; D001905:Botulinum Toxins