Botulinum neurotoxin type g proteolyses the ala81-Ala82 bond of rat synaptobrevin 2

Shinji Yamasaki, Thomas Binz, Tetsuya Hayashi, Elizabeth Szabo, Naomi Yamasaki, Mel Eklund, Reinharde Jahn, Heiner Niemann

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111 Citations (Scopus)


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 type 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.

Original languageEnglish
Pages (from-to)829-835
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Apr 30 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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