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How the widely used botulinum neurotoxin A (BoNT/A) recognizes and enters neurons is poorly understood. We found that BoNT/A enters neurons by binding to the synaptic vesicle protein SV2 (isoforms A, B, and C). Fragments of SV2 that harbor the toxin interaction domain inhibited BoNT/A from binding to neurons. BoNT/A binding to SV2A and SV2B knockout hippocampal neurons was abolished and was restored by expressing SV2A, SV2B, or SV2C. Reduction of SV2 expression in PC12 and Neuro-2a cells also inhibited entry of BoNT/A, which could be restored by expressing SV2 isoforms. Finally, mice that lacked an SV2 isoform (SV2B) displayed reduced sensitivity to BoNT/A. Thus, SV2 acts as the protein receptor for BoNT/A.
Authors : Dong Min , Yeh Felix , Tepp William H , Dean Camin , Johnson Eric A , Janz Roger , Chapman Edwin R ,
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WP2272: Pathogenic Escherichia coli infection
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WP1004: Kit Receptor Signaling Pathway
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WP1014: Androgen receptor signaling pathway
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WP1183: Toll-like receptor signaling pathway
WP1206: Signaling of Hepatocyte Growth Factor Receptor
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