The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a

Tei Ichi Nishiki, Yoshimi Tokuyama, Yoichi Kamata, Yasuo Nemoto, Akira Yoshida, Kazuki Sato, Mariko Sekiguchi, Masami Takahashi, Shunji Kozaki

Research output: Contribution to journalArticlepeer-review

208 Citations (Scopus)

Abstract

125I-labeled botulinum type B neurotoxin was shown to bind specifically to recombinant rat synaptotagmins I and II. Binding required reconstitution of the recombinant proteins with gangliosides GT1b/GD1a. Scatchard plot analyses revealed a single class of binding site with dissociation constants of 0.23 and 2.3 nM for synaptotagmin II and synaptotagmin I, respectively, values very similar to those of the high-(0.4 nM) and low-affinity (4.1 nM) binding sites in synaptosomes. The high-affinity binding of neurotoxin to synaptosomes was specifically inhibited by a monoclonal antibody recognizing with the amino-terminal region of synaptotagmin II. These results suggest that this region of synaptotagmin II participates in the formation of the high-affinity toxin binding site by associating with specific gangliosides.

Original languageEnglish
Pages (from-to)253-257
Number of pages5
JournalFEBS Letters
Volume378
Issue number3
DOIs
Publication statusPublished - Jan 15 1996

Keywords

  • Botulinum toxin
  • Ganglioside
  • Receptor
  • Synaptotagmin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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