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

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

doi:10.1016/0304-3940(93)90253-H

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 journal › Article › peer-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 language	English (US)
Pages (from-to)	159-162
Number of pages	4
Journal	Neuroscience letters
Volume	158
Issue number	2
DOIs	https://doi.org/10.1016/0304-3940(93)90253-H
State	Published - Aug 20 1993

All Science Journal Classification (ASJC) codes

General Neuroscience

Access to Document

10.1016/0304-3940(93)90253-H

Cite this

@article{6b134c540c194d6ca90257d671a9d14e,

title = "Ganglioside GD3 enhances adherence of botulinum and tetanus neurotoxins to bovine brain synapsin I",

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.",

author = "Schengrund, \{Cara Lynne\} and DasGupta, \{Bibhuti R.\} and Ringler, \{Nancy J.\}",

note = "Funding Information: This work was supported in part by Public Health Service Grants AI 23721 to C.-L.S. and NS17742 to B.R.DG. The authors thank Anne Stanley for carrying out the N-terminal amino acid sequence analyses.",

year = "1993",

month = aug,

day = "20",

doi = "10.1016/0304-3940(93)90253-H",

language = "English (US)",

volume = "158",

pages = "159--162",

journal = "Neuroscience letters",

issn = "0304-3940",

publisher = "Elsevier Ireland Ltd",

number = "2",

}

TY - JOUR

T1 - Ganglioside GD3 enhances adherence of botulinum and tetanus neurotoxins to bovine brain synapsin I

AU - Schengrund, Cara Lynne

AU - DasGupta, Bibhuti R.

AU - Ringler, Nancy J.

N1 - Funding Information: This work was supported in part by Public Health Service Grants AI 23721 to C.-L.S. and NS17742 to B.R.DG. The authors thank Anne Stanley for carrying out the N-terminal amino acid sequence analyses.

PY - 1993/8/20

Y1 - 1993/8/20

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0027162386

UR - https://www.scopus.com/pages/publications/0027162386#tab=citedBy

U2 - 10.1016/0304-3940(93)90253-H

DO - 10.1016/0304-3940(93)90253-H

M3 - Article

C2 - 8233089

AN - SCOPUS:0027162386

SN - 0304-3940

VL - 158

SP - 159

EP - 162

JO - Neuroscience letters

JF - Neuroscience letters

IS - 2

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this