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 Citations (Scopus)

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

Fingerprint

Tetanus Toxin
Diphtheria Toxin
Neurotoxins
Phospholipids
Membranes
Electric potential
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers. / Blaustein, Robert O.; Germann, William J.; Finkelstein, Alan; DasGupta, Bibhuti R.

In: FEBS Letters, Vol. 226, No. 1, 21.12.1987, p. 115-120.

Research output: Contribution to journalArticle

Blaustein, Robert O. ; Germann, William J. ; Finkelstein, Alan ; DasGupta, Bibhuti R. / The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers. In: FEBS Letters. 1987 ; Vol. 226, No. 1. pp. 115-120.
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