Snake and Spider Toxins Induce a Rapid Recovery of Function of Botulinum Neurotoxin Paralysed Neuromuscular Junction

Toxins (Basel). 2015 Dec 8;7(12):5322-36. doi: 10.3390/toxins7124887.

Abstract

Botulinum neurotoxins (BoNTs) and some animal neurotoxins (β-Bungarotoxin, β-Btx, from elapid snakes and α-Latrotoxin, α-Ltx, from black widow spiders) are pre-synaptic neurotoxins that paralyse motor axon terminals with similar clinical outcomes in patients. However, their mechanism of action is different, leading to a largely-different duration of neuromuscular junction (NMJ) blockade. BoNTs induce a long-lasting paralysis without nerve terminal degeneration acting via proteolytic cleavage of SNARE proteins, whereas animal neurotoxins cause an acute and complete degeneration of motor axon terminals, followed by a rapid recovery. In this study, the injection of animal neurotoxins in mice muscles previously paralyzed by BoNT/A or /B accelerates the recovery of neurotransmission, as assessed by electrophysiology and morphological analysis. This result provides a proof of principle that, by causing the complete degeneration, reabsorption, and regeneration of a paralysed nerve terminal, one could favour the recovery of function of a biochemically- or genetically-altered motor axon terminal. These observations might be relevant to dying-back neuropathies, where pathological changes first occur at the neuromuscular junction and then progress proximally toward the cell body.

Keywords: DAS assay; animal neurotoxins; botulinum neurotoxins; mouse; nerve terminals degeneration; neuroexocytosis; paralysis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Botulinum Toxins / toxicity*
  • Bungarotoxins / toxicity*
  • Male
  • Mice
  • Muscle, Skeletal / drug effects
  • Muscle, Skeletal / metabolism
  • Muscle, Skeletal / physiology
  • Neuromuscular Junction / drug effects
  • Neuromuscular Junction / metabolism
  • Neurotoxins / toxicity*
  • Snakes
  • Spider Venoms / toxicity*
  • Spiders
  • Synaptosomal-Associated Protein 25 / metabolism
  • Vesicle-Associated Membrane Protein 1 / metabolism

Substances

  • Bungarotoxins
  • Neurotoxins
  • Snap25 protein, mouse
  • Spider Venoms
  • Synaptosomal-Associated Protein 25
  • Vesicle-Associated Membrane Protein 1
  • vesicle-associated membrane protein 1, mouse
  • alpha-latrotoxin
  • Botulinum Toxins