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Ganglioside‐Induced Adherence of Botulinum and Tetanus Neurotoxins to Adducin
Author(s) -
Schengrund CaraLynne,
DasGupta Bibhuti R.,
Hughes Christine A.,
Ringler Nancy J.
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66062556.x
Subject(s) - neurotoxin , gel electrophoresis , ganglioside , synapsin i , biochemistry , clostridium botulinum , polyacrylamide gel electrophoresis , synapsin , chemistry , microbiology and biotechnology , biology , toxin , synaptic vesicle , enzyme , vesicle , membrane
Preincubation of botulinum neurotoxin serotype A, B, or E with ganglioside GT1b was previously found to enhance adherence of botulinum neurotoxin to synapsin I and an ∼116‐kDa bovine brain synaptosomal protein; in contrast, adherence to these two proteins by tetanus neurotoxin required preincubation with GT1b. We have now found that preincubation of the neurotoxins with ganglioside GD3 enhances their adherence to the ∼116‐kDa protein more than that with GT1b. A purified preparation of the water‐soluble ∼116‐kDa protein was obtained from bovine brain synaptosomes by preparative column sodium dodecyl sulfate‐polyacrylamide gel electrophoresis and two‐dimensional gel electrophoresis. N‐Terminal amino acid sequences were obtained for two tryptic fragments of the ∼116‐kDa protein. These sequences matched with the data bank sequences for β‐adducin, a cytoskeletal protein. The carboxy‐terminal tail region of adducin, but not the head region, was adhered to by the neurotoxins. Adherence of the neurotoxin to adducin and synapsin I may facilitate presentation of the neurotoxin to its specific substrate(s).