Tyrosine-1290 of tetanus neurotoxin plays a key role in its binding to gangliosides and functional binding to neurones

J. Mark Sutton, Oliver Chow-Worn, Lindsey Spaven, Nigel Silman, Bassam Hallis, Clifford Shone*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)

Abstract

Tetanus toxin acts by blocking the release of glycine from inhibitory neurones within the spinal cord. An initial stage in the toxin's action is binding to acceptors on the nerve surface and polysialogangliosides are a component of these acceptor moieties. Using site-directed mutagenesis, we identify tyrosine-1290 of tetanus toxin as a key residue that is involved in ganglioside binding. This residue, which is located at the centre of a shallow pocket on the β-trefoil domain of the tetanus Hc fragment, is also shown to play a key role in the functional binding of tetanus toxin to spinal cord neurones leading to the inhibition of neurotransmitter release.

Original languageEnglish
Pages (from-to)45-49
Number of pages5
JournalFEBS Letters
Volume493
Issue number1
DOIs
Publication statusPublished - 23 Mar 2001

Bibliographical note

Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.

Keywords

  • Botulinum
  • Ganglioside
  • Motoneuron
  • Neurotoxin
  • Receptor
  • Tetanus

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