Synaptic vesicle glycoprotein 2 isoform (SV2A, SV2B, SV2C) (SV2A, SV2B, SV2C)

Synaptic vesicle glycoprotein 2 isoforms (SV2A, SV2B, SV2C) are integral membrane proteins found on the surface of all synaptic vesicles in vertebrates[3][5][6]. Structurally, SV2 proteins belong to the major facilitator superfamily (MFS), possessing 12 transmembrane domains, and are highly glycosylated with large N-glycosylated intraluminal loops[3][5]. SV2A is the predominant isoform in the brain and serves as the binding site for the antiepileptic drugs levetiracetam and brivaracetam[2][6]. The family also acts as the neuronal receptor for several botulinum neurotoxin serotypes[4][5][8]. SV2 proteins modulate neurotransmitter release by influencing vesicle exocytosis, priming, and synaptotagmin availability, but their precise molecular role remains incompletely defined[5][9]. Loss of SV2A activity disrupts synaptic transmission and results in severe seizures and early mortality in animal models[7]. Altered SV2 expression or function has been implicated in epilepsy, neurodegenerative diseases, and as a route for neurotoxin entry in botulism[6][8].

Other names

SV2 (original discovery)Synaptic vesicle glycoprotein 2A/B/CSV2A/B/C

Levetiracetam/Brivaracetam: Bind SV2A, modulating neurotransmitter release and vesicular trafficking. Botulinum neurotoxin: Binds extracellular (luminal) domain of SV2 isoforms to enter neurons and block neurotransmission.