Discovery of a novel enzymatic cleavage site for botulinum neurotoxin F5

FEBS Lett. 2012 Jan 20;586(2):109-15. doi: 10.1016/j.febslet.2011.11.033. Epub 2011 Dec 9.

Abstract

Botulinum neurotoxins (BoNTs) cause botulism by cleaving proteins necessary for nerve transmission. There are seven serotypes of BoNT, A-G, characterized by their response to antisera. Many serotypes are further distinguished into differing subtypes based on amino acid sequence, some of which result in functional differences. Our laboratory previously reported that all tested subtypes within each serotype have the same site of enzymatic activity. Recently, three new subtypes of BoNT/F; /F3, /F4, and /F5, were reported. Here, we report that BoNT/F5 cleaves substrate synaptobrevin-2 in a different location than the other BoNT/F subtypes, between (54)L and (55)E. This is the first report of cleavage of synaptobrevin-2 in this location.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Botulinum Toxins / chemistry*
  • Botulinum Toxins / genetics
  • Botulinum Toxins / metabolism*
  • Catalytic Domain / genetics
  • Cloning, Molecular
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Hydrolases / chemistry
  • Peptide Hydrolases / genetics
  • Peptide Hydrolases / metabolism
  • Protein Interaction Domains and Motifs* / genetics
  • Protein Interaction Maps
  • Proteolysis*
  • Substrate Specificity / genetics
  • Vesicle-Associated Membrane Protein 2 / chemistry
  • Vesicle-Associated Membrane Protein 2 / metabolism*

Substances

  • Vesicle-Associated Membrane Protein 2
  • Peptide Hydrolases
  • Botulinum Toxins
  • botulinum toxin type F