Ganglioside GD3 enhances adherence of botulinum and tetanus neurotoxins to bovine brain synapsin I.
Tetanus toxin (TTx) and botulinum toxin serotype A (BTxA), preincubated with trisialoganglioside GT1b, adhere to proteins present on blots of bovine synaptosomal proteins. Differential solubilization and ammonium sulfate fractionation provided material enriched in two proteins that appeared to be adhered to most strongly by the labeled neurotoxins. After excision of the appropriate bands from blots of electrophoretically separated proteins, N-terminal amino acid sequence analysis permitted identification of the proteins as synapsins Ia and Ib. Comparison of the effectiveness of different gangliosides at enhancing adherence of the neurotoxins to blots of synapsins Ia and Ib indicated that GD3 was most effective.
Schengrund
C L
CL
Department of Biological Chemistry, Milton S. Hershey Medical Center, Pennsylvania State University, Hershey 17033.
DasGupta
B R
BR
Ringler
N J
NJ
D000595:Amino Acid Sequence; D000645:Ammonium Sulfate; D000818:Animals; D001905:Botulinum Toxins / Q000276:immunology / Q000378:metabolism*; D002417:Cattle; D005732:Gangliosides / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000276:immunology / Q000378:metabolism*; D011485:Protein Binding; D016704:Synapsins / Q000276:immunology / Q000378:metabolism*; D013744:Tetanus Toxin / Q000276:immunology / Q000378:metabolism*
D005732:Gangliosides; D009498:Neurotoxins; D016704:Synapsins; D013744:Tetanus Toxin; C026226:ganglioside, GD3; D001905:Botulinum Toxins; D000645:Ammonium Sulfate