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Incorporation of protease K into larval insect membrane vesicles does not result in disruption of integrity or function of the pore-forming Bacillus thuringiensis delta-endotoxin.

作者信息

Aronson A

机构信息

Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA.

出版信息

Appl Environ Microbiol. 2000 Oct;66(10):4568-70. doi: 10.1128/AEM.66.10.4568-4570.2000.

Abstract

Bacillus thuringiensis delta-endotoxins insert into the brush border membranes of insect larval cells to form ion channels. A possible interaction of these toxins with a cytoplasmic component was examined by preloading vesicles from insect larval cells with protease K followed by incubation with toxin. There was no evidence for toxin antigens smaller than the intact toxin in extracts of solubilized vesicles, nor was there an effect of the inclusion of protease K on either of two functional properties, the formation of toxin aggregates or of ion pores. These toxins, physically and functionally, appear to be confined to the membrane.

摘要

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本文引用的文献

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Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel.
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3
Aggregation of bacillus thuringiensis Cry1A toxins upon binding to target insect larval midgut vesicles.
Appl Environ Microbiol. 1999 Jun;65(6):2503-7. doi: 10.1128/AEM.65.6.2503-2507.1999.
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Bacillus thuringiensis and its pesticidal crystal proteins.
Microbiol Mol Biol Rev. 1998 Sep;62(3):775-806. doi: 10.1128/MMBR.62.3.775-806.1998.
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The two faces of Bacillus thuringiensis: insecticidal proteins and post-exponential survival.
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