Benjamin Spiller
Last active: 2/25/2021

Structural analysis of botulinum neurotoxin type G receptor binding .

Schmitt J, Karalewitz A, Benefield DA, Mushrush DJ, Pruitt RN, Spiller BW, Barbieri JT, Lacy DB
Biochemistry. 2010 49 (25): 5200-5

PMID: 20507178 · PMCID: PMC2894633 · DOI:10.1021/bi100412v

Botulinum neurotoxin (BoNT) binds peripheral neurons at the neuromuscular junction through a dual-receptor mechanism that includes interactions with ganglioside and protein receptors. The receptor identities vary depending on BoNT serotype (A-G). BoNT/B and BoNT/G bind the luminal domains of synaptotagmin I and II, homologous synaptic vesicle proteins. We observe conditions under which BoNT/B binds both Syt isoforms, but BoNT/G binds only SytI. Both serotypes bind ganglioside G(T1b). The BoNT/G receptor-binding domain crystal structure provides a context for examining these binding interactions and a platform for understanding the physiological relevance of different Syt receptor isoforms in vivo.

MeSH Terms (8)

Botulinum Toxins Crystallography, X-Ray Gangliosides Genetic Vectors Models, Molecular Protein Binding Protein Conformation Receptors, Cell Surface

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