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

doi:10.1016/0014-5793(87)80562-8

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

Physiology & Biophysics

Research output: Contribution to journal › Article › peer-review

95 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 language	English (US)
Pages (from-to)	115-120
Number of pages	6
Journal	FEBS Letters
Volume	226
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(87)80562-8
State	Published - 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

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10.1016/0014-5793(87)80562-8

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

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.",

keywords = "(Clostridium botulinum), Diphtheria toxin, Lipid bilayer, Neurotoxin fragment, Tetanus toxin, Voltage gating, pH-dependent channel",

author = "Blaustein, {Robert O.} and Germann, {William J.} and Alan Finkelstein and DasGupta, {Bibhuti R.}",

note = "Funding Information: We thank V. Sathyamoorthya nd J. Foley jr for their assistancein preparingt he neurotoxina nd its fragments, and Professor Azer Lektin for a stimulatingd iscussion.T his work was supported by NIH grantsG M29210-10( A.F.), NS17742a nd NS24545 (B.R.D.), NIH Training grant T32GM7288f rom NIGMS (R.O.B.), and the Food ResearchI nstitutea nd College of Agriculture and Life Sciences of the University of Wisconsin (B.R.D.).",

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doi = "10.1016/0014-5793(87)80562-8",

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T1 - The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers

AU - Blaustein, Robert O.

AU - Germann, William J.

AU - Finkelstein, Alan

AU - DasGupta, Bibhuti R.

N1 - Funding Information: We thank V. Sathyamoorthya nd J. Foley jr for their assistancein preparingt he neurotoxina nd its fragments, and Professor Azer Lektin for a stimulatingd iscussion.T his work was supported by NIH grantsG M29210-10( A.F.), NS17742a nd NS24545 (B.R.D.), NIH Training grant T32GM7288f rom NIGMS (R.O.B.), and the Food ResearchI nstitutea nd College of Agriculture and Life Sciences of the University of Wisconsin (B.R.D.).

PY - 1987/12/21

Y1 - 1987/12/21

N2 - 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.

AB - 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.

KW - (Clostridium botulinum)

KW - Diphtheria toxin

KW - Lipid bilayer

KW - Neurotoxin fragment

KW - Tetanus toxin

KW - Voltage gating

KW - pH-dependent channel

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

Abstract

Keywords

ASJC Scopus subject areas

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