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PMID: 2445378 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Escherichia coli haemolysin forms voltage-dependent ion channels in lipid membranes.

Biochimica et biophysica acta ·Vol. 905 ·No. 1 ·1987-11-27 ·Pages 109-17

Menestrina G, Mackman N, Holland IB, Bhakdi S

Abstract

The action of the 107 kDa hemolysin from Escherichia coli on planar lipid membranes was investigated. We report that a single toxin molecule can form a cation-selective, ion-permeable channel of large conductance in a planar phospholipid bilayer membrane. The conductance of the pore is proportional to that of the bulk solution, indicating that the channel is filled with water. A pore diameter of about 2 nm can be evaluated. The pore formation mechanism is voltage-dependent and essentially resembles that of pore-forming colicins; this implies that opening of the channel is dependent on transfer of an electrical charge through the membrane. We propose that the physiological effects of E. coli hemolysin result from its ability to form ion channels in the membrane of attacked cells, and show that there is quantitative agreement between the effects of this toxin on model membranes and its hemolytic properties.

MeSH Terms
Calcium/metabolism Escherichia coli/analysis Hemolysin Proteins/isolation & purification,pharmacology Ion Channels/drug effects Lipid Bilayers/metabolism Membrane Potentials Peptide Hydrolases/pharmacology Phospholipids Potassium/metabolism Sodium/metabolism
Chemicals
Hemolysin Proteins Ion Channels Lipid Bilayers Phospholipids Sodium Peptide Hydrolases Potassium Calcium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Menestrina G
Department of Physics, University of Trento, Povo, Italy.
Mackman N
Holland I B
Bhakdi S
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1987-11-27
Pages
109-17
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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