Structural Analysis of Botulinum Neurotoxin Type G Receptor Binding

Journal Article · Tue Oct 19 04:00:00 EDT 2010 · Biochemistry-US

DOI:https://doi.org/10.1021/bi100412v· OSTI ID:1002761

Schmitt, John; Karalewitz, Andrew; Benefield, Desire A; Mushrush, Darren J; Pruitt, Rory N; Spiller, Benjamin W; Barbieri, Joseph T; Lacy, D Borden ^[1]

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1. Vanderbilt

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{sub 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.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1002761
• Journal Information: Biochemistry-US, Journal Name: Biochemistry-US Journal Issue: (25) ; 06, 2010 Vol. 49; ISSN 0006-2960; ISSN 1520-4995; ISSN BICHAW
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

36 MATERIALS SCIENCE
CRYSTAL STRUCTURE
GANGLIOSIDES
IN VIVO
NERVE CELLS
PHENOBARBITAL
PROTEINS