Glycosphingolipids-sweets for botulinum neurotoxin

A number of viruses, bacteria, and bacterial toxins can only act on cells that express the appropriate glycosphingolipids (GSLs) on the outer surface of their plasma membranes. An example of this dependency is provided by botulinum neurotoxin (BoNT) which is synthesized by Clostridium botulinum and...

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Bibliographic Details
Published in:Glycoconjugate journal 2004-01, Vol.21 (6), p.287-293
Main Authors: Yowler, Brian C, Schengrund, Cara-Lynne
Format: Article
Language:English
Subjects:
Botulinum Toxins, Type A - metabolism
Botulism
Carbohydrate Sequence
Clostridium botulinum
Glycosphingolipids - chemistry
Glycosphingolipids - metabolism
Glycosphingolipids - physiology
Molecular Sequence Data
Protein Binding
Proteins
Surface Plasmon Resonance
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Summary:A number of viruses, bacteria, and bacterial toxins can only act on cells that express the appropriate glycosphingolipids (GSLs) on the outer surface of their plasma membranes. An example of this dependency is provided by botulinum neurotoxin (BoNT) which is synthesized by Clostridium botulinum and inhibits neurotransmission at the neuromuscular junction by catalyzing hydrolysis of a SNARE protein, thereby inducing a flaccid paralysis. Haemagglutinin components of progenitor forms of BoNT mediate its adherence to glycosphingolipids (GSLs) on intestinal epithelial cells while the cellular activity of most isolated serotypes requires the presence of certain gangliosides, especially those of the Gg1b family. This review discusses available information about the identity and the roles of GSLs in the activity of BoNT. Observations that serotypes A-F of BoNT require gangliosides for optimum activity (serotype G apparently does not), permits the hypothesis that it should be possible to develop an antagonist of this interaction thereby inhibiting/reducing its effect.
ISSN:0282-0080
1573-4986
DOI:10.1023/B:GLYC.0000046271.64647.fd