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PMID: 7556616 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interaction of the bacterial protein toxin alpha-haemolysin with model membranes: protein binding does not always lead to lytic activity.

FEBS letters ·Vol. 371 ·No. 3 ·1995-09-11 ·Pages 303-6

Ostolaza H, Goñi FM

Abstract

alpha-Haemolysin interaction with model membranes has been investigated by a 2-fold procedure. First, protein binding has been measured, by a direct method as well as through changes in the intrinsic fluorescence of the protein when incubated with liposomes and divalent cations. Then, the above results have been correlated with the protein lytic activity. The extent of protein binding is not significantly modified by the presence or absence of Ca2+, or by changes in lipid composition, although these factors influence greatly the membrane lytic activity of the protein. Moreover, Ca2+ binding to the toxin must occur prior to protein binding to the bilayer, for a lytic effect to take place.

MeSH Terms
Bacterial Proteins/metabolism Bacterial Toxins/metabolism Cations, Divalent Escherichia coli Proteins Hemolysin Proteins/metabolism Liposomes/metabolism Membrane Lipids/metabolism Protein Binding
Chemicals
Bacterial Proteins Bacterial Toxins Cations, Divalent Escherichia coli Proteins Hemolysin Proteins Hlya protein, E coli Liposomes Membrane Lipids
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ostolaza H
Department of Biochemistry, University of the Basque Country, Bilbao, Spain.
Goñi F M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1995-09-11
Pages
303-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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