Recombinant luminal domain of human synaptotagmin II in combination with gangliosides inhibits the toxicity of botulinum neurotoxins in mice |
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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 |
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| Institution: | 1. Histology and Molecular Biology Section Army Medical and Veterinary Research Center, Rome, Italy;2. National Reference Center for Botulism, Department of Veterinary Public Health and Food Safety, Istituto Superiore di Sanità (ISS), Rome, Italy |
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| 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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