Lipid-induced pore formation of the Bacillus thuringiensis Cry1Aa insecticidal toxin

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DOIResolve DOI: http://doi.org/10.1007/s002320010070
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TypeArticle
Journal titleJournal of Membrane Biology
Volume180
Issue3
Pages195203; # of pages: 9
Subjectenv; Lipid monolayers; Protein insertion; Cry1Aa toxin; Amphipathic properites; Pore formation
AbstractAfter activation, Bacillus thuringiensis (Bt) insecticidal toxin forms pores in larval midgut epithelial cell membranes, leading to host death. Although the crystal structure of the soluble form of Cry1Aa has been determined, the conformation of the pores and the mechanism of toxin interaction with and insertion into membranes are still not clear. Here we show that Cry1Aa spontaneously inserts into lipid mono- and bilayer membranes of appropriate compositions. Fourier Transform InfraRed spectroscopy (FTIR) indicates that insertion is accompanied by conformational changes characterized mainly by an unfolding of the b-sheet domains. Moreover, Atomic Force Microscopy (AFM) imaging strongly suggests that the pores are composed of four subunits surrounding a 1.5 nm diameter central depression
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number44594
NPARC number3539019
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Record identifiera48ac178-bf49-4877-b7ca-b5df4f905c50
Record created2009-03-01
Record modified2016-05-09
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