Ganglioside GD3 enhances adherence of botulinum and tetanus neurotoxins to bovine brain synapsin I

Cara Lynne Schengrund, Bibhuti R. DasGupta, Nancy J. Ringler

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)159-162
Number of pages4
JournalNeuroscience letters
Volume158
Issue number2
DOIs
StatePublished - Aug 20 1993

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

Fingerprint Dive into the research topics of 'Ganglioside GD3 enhances adherence of botulinum and tetanus neurotoxins to bovine brain synapsin I'. Together they form a unique fingerprint.

  • Cite this