title: Glycosphingolipids-sweets for botulinum neurotoxin.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology H171, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.
authors.forename: Brian C
authors.initials: BC
authors.lastname: Yowler
authors.forename: Cara-Lynne
authors.initials: CL
authors.lastname: Schengrund
mesh_terms: D019274:Botulinum Toxins, Type A / Q000378:metabolism*; D002240:Carbohydrate Sequence; D006028:Glycosphingolipids / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D008969:Molecular Sequence Data; D011485:Protein Binding; D020349:Surface Plasmon Resonance
chemical_list: D006028:Glycosphingolipids; D019274:Botulinum Toxins, Type A