NDLI: Synaptotagmin II and gangliosides bind independently with botulinum neurotoxin B but each restrains the other.

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Synaptotagmin II and gangliosides bind independently with botulinum neurotoxin B but each restrains the other.

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Synaptotagmin II and gangliosides bind independently with botulinum neurotoxin B but each restrains the other.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Atassi, M. Zouhair Taruishi, Midori Naqvi, Masooma Steward, Lance E. Aoki, K. Roger
Description	Author Affiliation: Atassi MZ ( Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX, 77030, USA, matassi@bcm.edu.)
Abstract	Botulinum neurotoxin type B (BoNT/B) initiates its toxicity by binding to synaptotagmin II (SytII) and gangliosides GD1a and GT1b on the neural membrane. We synthesized two 27-residue peptides that carry the BoNT/B binding sites on mouse SytII (mSytII 37-63) or human SytII (hSytII 34-60). BoNT/B bound to these peptides, but showed substantially higher binding to mSytII peptide than to hSytII peptide. The mSytII peptide inhibited almost completely BoNT/B binding to synaptosomes (snps) and displayed a high affinity. BoNT/B bound strongly to mSytII peptide and binding was inhibited by the peptide. Binding of BoNT/B to snps was also inhibited (~80 %) by a larger excess of gangliosides GD1a or GT1b. The mSytII peptide inhibited very strongly (at least 80 %) the toxin binding to snps, while the two gangliosides were much less efficient inhibitors requiring much larger excess to achieve similar inhibition levels. Furthermore, gangliosides GD1a or GT1b inhibited BoNT/B binding to mSytII peptide at a much larger excess than the inhibition by mSytII peptide. Conversely, BoNT/B bound well to each ganglioside and binding could be inhibited by the correlate ganglioside and much less efficiently by the mSytII peptide. There was no apparent collaboration between mSytII peptide and either ganglioside. mSytII peptide displayed some protective activity in vivo in mice against a lethal BoNT/B dose. We concluded that SytII peptide and gangliosides bind independently but, with their binding sites on BoNT/B being spatially close, each can influence BoNT/B binding to the other due to regional conformational perturbations or steric interference or both. Ganglioside involvement in BoNT/B binding might help in toxin translocation and endocytosis.
File Format	HTM / HTML
ISSN	15723887
Issue Number	3
Volume Number	33
e-ISSN	15734943
Journal	The Protein Journal
Language	English
Publisher	Springer
Publisher Date	2014-06-01
Publisher Place	Netherlands
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Botulinum Toxins Metabolism Gangliosides Synaptotagmin Ii Animals Chemistry Botulinum Toxins, Type A Humans Iodine Radioisotopes Mice Models, Molecular Peptides Protein Binding Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Organic Chemistry Analytical Chemistry Biochemistry Bioengineering

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