Synaptic vesicle glycoprotein 2C–ganglioside GT1b complex (SV2C/GT1b complex)

SV2C/GT1b complex refers to the functional receptor platform formed by **synaptic vesicle glycoprotein 2C (SV2C)** and **ganglioside GT1b** present on the surface of presynaptic cholinergic neurons. This dual-receptor complex is essential for the high-affinity binding and internalization of botulinum neurotoxin A (BoNT/A), which utilizes both carbohydrate (GT1b) and protein (SV2C) interactions for selective neuronal uptake. SV2C is a transmembrane glycoprotein with an important role in synaptic vesicle trafficking and neurotransmitter release regulation, while GT1b is a sialic acid-rich ganglioside that contributes to membrane microdomain formation and initial toxin docking. The complex is key to the pharmacological action of BoNT/A as a neuroparalytic agent and is regionally expressed in the brain, with implications for both therapeutic use and neurotoxicity in diseases such as botulism[1][2][3][4][5][6].

Other names

SV2C/GT1b receptor complexSV2C–GT1b

High-affinity binding of neurotoxin heavy chain (BoNT/A-HC) to both SV2C and GT1b mediates endocytosis\nEndosomal acidification triggers conformational change and translocation of toxin light chain\nThe light chain cleaves SNAP25, blocking neurotransmitter release