| DOI | Resolve DOI: https://doi.org/10.1007/s002320010070 |
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| Author | Search for: Vié, V.; Search for: Van Mau, N.; Search for: Pomarède, P.; Search for: Dance, C.; Search for: Schwartz, J. L.1; Search for: Laprade, R.; Search for: Frutos, R.; Search for: Rang, C.; Search for: Masson, L.1; Search for: Heitz, F.; Search for: Le Grimellec C. |
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| Affiliation | - National Research Council of Canada. NRC Biotechnology Research Institute
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| Format | Text, Article |
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| Subject | environmental; Lipid monolayers; Protein insertion; Cry1Aa toxin; Amphipathic properites; Pore formation |
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| Abstract | After 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 |
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| Publication date | 2001 |
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| In | |
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| Language | English |
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| NRC number | 44594 |
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| NPARC number | 3539019 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | a48ac178-bf49-4877-b7ca-b5df4f905c50 |
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| Record created | 2009-03-01 |
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| Record modified | 2020-03-27 |
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