The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers

Robert O. Blaustein, William J. Germann, Alan Finkelstein, Bibhuti R. DasGupta

Research output: Contribution to journalArticle

91 Scopus citations

Abstract

The heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayer membranes. Channel activity is confined to the N-terminal half of this chain; the C-terminal half is inactive. Channel activity is stimulated by low pH (4.5-5.5) on the cis side (the side to which protein is added), neutral pH on the opposite (trans) side, and cis positive voltages. These findings are strikingly similar to those previously reported for analogous fragments of diphtheria and tetanus toxins.

Original languageEnglish (US)
Pages (from-to)115-120
Number of pages6
JournalFEBS Letters
Volume226
Issue number1
DOIs
StatePublished - Dec 21 1987

Keywords

  • (Clostridium botulinum)
  • Diphtheria toxin
  • Lipid bilayer
  • Neurotoxin fragment
  • Tetanus toxin
  • Voltage gating
  • pH-dependent channel

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers'. Together they form a unique fingerprint.

  • Cite this