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Recombinant luminal domain of human synaptotagmin II in combination with gangliosides inhibits the toxicity of botulinum neurotoxins in mice

  • Jing Shi
  • , Tao Li
  • , Xiaojun Hou
  • , Kun Cai
  • , Shizhong Bao
  • , Hao Liu
  • , Xiang Gao
  • , Le Xiao
  • , Wei Tu
  • , Qin Wang
  • , Jun Yin
  • , Hui Wang*
  • *Corresponding author for this work
  • Academy of Military Medical Science China

Research output: Contribution to journalArticlepeer-review

Abstract

Synaptotagmin II (syt II) is the specific protein receptor of botulinum neurotoxin B (BoNT/B), and the luminal domain of syt II contains toxin-binding sites that have a high affinity for BoNT/B. However, it is not yet clear whether the luminal domain of syt II (syt II-LD) inhibits the toxicity of BoNT/B by interfering with the toxin-receptor interaction. In this study, we characterized the binding of the purified recombinant syt II-LD to BoNT and revealed that the recombinant syt II-LD in vivo could provide protection against BoNT/B intoxication in mice models, and the neutralization effect could be improved by using gangliosides.

Original languageEnglish
Pages (from-to)319-323
Number of pages5
JournalMicrobes and Infection
Volume12
Issue number4
DOIs
StatePublished - Apr 2010
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • Botulinum neurotoxin
  • Ganglioside
  • Receptor
  • Synaptotagmin

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