Haider M Z, Ellar D J
University of Cambridge, Department of Biochemistry, U.K.
Biochim Biophys Acta. 1989 Jan 30;978(2):216-22. doi: 10.1016/0005-2736(89)90118-1.
Bacillus thuringiensis (Bt) crystal delta-endotoxin from three subspecies and the product of a cloned crystal protein gene were activated in vitro and their interaction with phospholipid liposomes studied. Despite their diverse spectrum of activity, all these toxins were found to cause a rapid increase in the light scattering of liposome suspensions, which reflects a morphological change in the lipid bilayer. When liposomes loaded with radioactive markers were incubated with B. thuringiensis aizawai IC1 toxin, a relatively rapid release of more than 70% of the trapped markers occurred after an initial lag. Activated Bta IC1 and B. thuringiensis israelensis toxins were shown to bind to phospholipid vesicles. Two of the five conserved domains (D1-D5) detectable in the sequence of a range of Bt toxins are predicted to be highly hydrophobic. It is suggested that these, together with an additional conserved hydrophobic region showing structural homology and two predicted amphiphilic helices, play a major part in the interaction of these toxins with target membranes.
