TY - JOUR
T1 - Ganglioside-induced adherence of botulinum and tetanus neurotoxins to adducin
AU - Schengrund, Cara Lynne
AU - DasGupta, Bibhuti R.
AU - Hughes, Christine A.
AU - Ringler, Nancy J.
PY - 1996/6
Y1 - 1996/6
N2 - 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).
AB - 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).
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U2 - 10.1046/j.1471-4159.1996.66062556.x
DO - 10.1046/j.1471-4159.1996.66062556.x
M3 - Article
C2 - 8632182
AN - SCOPUS:0029950636
SN - 0022-3042
VL - 66
SP - 2556
EP - 2561
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
IS - 6
ER -