| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3415283 | Microbes and Infection | 2010 | 5 Pages |
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.
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Authors
Jing Shi, Tao Li, Xiaojun Hou, Kun Cai, Shizhong Bao, Hao Liu, Xiang Gao, Le Xiao, Wei Tu, Qin Wang, Jun Yin, Hui Wang,
