Endocytosis, trafficking and exocytosis of intact full-length botulinum neurotoxin type a in cultured rat neurons.

ABSTRACT: Botulinum toxin A (BoNT/A) is a potent neurotoxin that acts primarily by silencing synaptic transmission by blocking neurotransmitter release. BoNT/A comprises a light chain (LC/A) intracellular protease and a heavy chain (HC/A) composed of a receptor binding domain (HC_C/A) and a translocation domain (HC_N/A) that mediates cell entry. Following entry into the neuron, the disulphide bond linking the two peptide chains is reduced to release the LC/A. To gain better insight into the trafficking and fate of BoNT/A before dissociation we have used a catalytically inactive, non-toxic full-length BoNT/A(0) mutant. Our data confirm that BoNT/A(0) enters cortical neurons both in an activity-dependent manner and via a pathway dependent on fibroblast growth factor receptor 3 (Fgf

SUBMITTER: Solabre Valois L 

PROVIDER: S-EPMC7225749 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature