Characterization of clostridium botulinum neurotoxin serotype A (BoNT/A) and fibroblast growth factor receptor interactions using novel receptor dimerization assay.

ABSTRACT: Clostridium botulinum neurotoxin serotype A (BoNT/A) is a potent neurotoxin that serves as an effective therapeutic for several neuromuscular disorders via induction of temporary muscular paralysis. Specific binding and internalization of BoNT/A into neuronal cells is mediated by its binding domain (H_C/A), which binds to gangliosides, including GT1b, and protein cell surface receptors, including SV2. Previously, recombinant H_C/A was also shown to bind to FGFR3. As FGFR dimerization is an indirect measure of ligand-receptor binding, an FCS & TIRF receptor dimerization assay was developed to measure rH_C/A-induced dimerization of fluorescently tagged FGFR subtypes (FGFR1-3) in cells. rH_C/A dimerized FGFR subtypes in the rank order FGFR3c (EC_50<

SUBMITTER: James NG 

PROVIDER: S-EPMC8035261 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature