Publication: Structure and distribution of the Bacillus thuringiensis Cry4Ba toxin in lipid membranes
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Issued Date
2005-11-01
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ISSN
03043991
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2-s2.0-27544465807
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Mahidol University
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SCOPUS
Bibliographic Citation
Ultramicroscopy. Vol.105, No.1-4 (2005), 115-124
Suggested Citation
Theeraporn Puntheeranurak, Cordula Stroh, Rong Zhu, Chanan Angsuthanasombat, Peter Hinterdorfer Structure and distribution of the Bacillus thuringiensis Cry4Ba toxin in lipid membranes. Ultramicroscopy. Vol.105, No.1-4 (2005), 115-124. doi:10.1016/j.ultramic.2005.06.026 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/16624
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Title
Structure and distribution of the Bacillus thuringiensis Cry4Ba toxin in lipid membranes
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Abstract
Bacillus thuringiensis Cry δ-endotoxins cause death of susceptible insect larvae by forming lytic pores in the midgut epithelial cell membranes. The 65 kDa trypsin activated Cry4Ba toxin was previously shown to be capable of permeabilizing liposomes and forming ionic channels in receptor-free planar lipid bilayers. Here, magnetic ACmode (MACmode) atomic force microscopy (AFM) was used to characterize the lateral distribution and the native molecular structure of the Cry4Ba toxin in the membrane. Liposome fusion and the Langmuir-Blodgett technique were employed for supported lipid bilayer preparations. The toxin preferentially inserted in a self-assembled structure, rather than as a single monomeric molecule. In addition, the spontaneous insertion into receptor-free lipid bilayers lead to formation of characteristic pore-like structures with four-fold symmetry, suggesting that tetramers are the preferred oligomerization state of this toxin. © 2005 Elsevier B.V. All rights reserved.