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 journalArticlepeer-review

    12 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

    • General Neuroscience

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