Botulinum neurotoxin type G proteolyses the Ala81-Ala82 bond of rat synaptobrevin 2

Biochem Biophys Res Commun. 1994 Apr 29;200(2):829-35. doi: 10.1006/bbrc.1994.1526.

Abstract

Tetanus toxin and the botulinum neurotoxins types A to F inhibit neurotransmitter release from presynaptic nerve endings by selectively proteolysing the synaptic proteins synaptobrevin, syntaxin, or SNAP-25. Here, we show that botulinum toxin type G cleaves rat synaptobrevin 2 between Ala81 and Ala82, a peptide bond that differs from those attacked by tetanus toxin and the botulinal toxins types B, D, and F. Synaptobrevin isoforms carrying a Gly in the P1 position are poor substrates. Analyses of N-terminal deletion mutants of rat synaptobrevin 2 showed that a substrate starting at Leu54 is cleaved efficiently, whereas substrates beginning at Leu60 or Phe77 are cleaved partially or not at all, respectively.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites / genetics
  • Botulinum Toxins / chemistry
  • Botulinum Toxins / genetics
  • Botulinum Toxins / toxicity*
  • DNA Primers / genetics
  • Endopeptidases / chemistry
  • Endopeptidases / genetics
  • Endopeptidases / toxicity
  • In Vitro Techniques
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Molecular Sequence Data
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism*
  • Neurotransmitter Agents / metabolism
  • Protein Conformation
  • R-SNARE Proteins
  • Rats
  • Sequence Deletion
  • Substrate Specificity
  • Synaptic Vesicles / drug effects
  • Synaptic Vesicles / physiology

Substances

  • DNA Primers
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Neurotransmitter Agents
  • R-SNARE Proteins
  • Endopeptidases
  • Botulinum Toxins