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J. Biol. Chem., Vol. 269, Issue 44, 27231-27239, 11, 1994
R Benz, E Maier, D Ladant, A Ullmann and P Sebo
The interaction between the adenylate cyclase toxin (CyaA) of Bordetella
pertussis and lipid was studied using the lipid bilayer assay. The addition
of CyaA to the aqueous phase bathing lipid bilayer membranes composed of
different lipids resulted in the increase of the membrane conductance. This
increase was rather small for membranes formed of pure lipids as compared
with lipid mixtures such as asolectin. The toxin formed in asolectin
membranes small transient ion- permeable channels with a single-channel
conductance of 27 pS in 1 M KCl, which is considerably smaller than that of
the alpha-hemolysin (HlyA) of Escherichia coli (1500 pS). Experiments with
different salts suggested that the CyaA-induced channels were exclusively
cation- selective because of negative charges localized at the channel
mouth. The single-channel conductance of channels initiated by CyaA was
independent of whether the toxin was purified from B. pertussis or from
recombinant E. coli. However, the channel-forming activity of the CyaA
expressed in B. pertussis was substantially higher than that of the
recombinant toxin. Experiments with mutant forms of CyaA suggested that
both the activation of CyaA by CyaC and the hemeolytic part of the toxin,
but not the repeats and the cyclase activity, are required for channel
formation in lipid bilayer membranes.
Adenylate cyclase toxin (CyaA) of Bordetella pertussis. Evidence for the formation of small ion-permeable channels and comparison with HlyA of Escherichia coli
Lehrstuhl fur Biotechnologie, Theodor-Boveri-Institut (Biozentrum), Universitat Wurzburg, Federal Republic of Germany.
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