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

FEBS Letters

Blaustein, Robert O.¹  Finkelstein, Alan¹  Germann, William J.¹  DasGupta, Bibhuti R.² 

[1] Departments of Physiology and Biophysics and Neuroscience, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA;Food Research Institute, University of Wisconsin, 1925 Willow Drive, Madison, WI 53706, USA

关键词: Neurotoxin fragment;    pH-dependent channel;    Voltage gating;    Lipid bilayer;    Diphtheria toxin;    Tetanus toxin;    (Clostridium botulinum);   

DOI  :  10.1016/0014-5793(87)80562-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown