publication . Article . 2006

Effects of Disulfide Bridges in Domain I of Bacillus thuringiensis Cry1Aa δ-Endotoxin on Ion-Channel Formation in Biological Membranes

O. Alzate; T. You; M. Claybon; C. Osorio; A. Curtiss; D. H. Dean;
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  • Published: 21 Oct 2006 Journal: Biochemistry, volume 45, pages 13,597-13,605 (issn: 0006-2960, eissn: 1520-4995, Copyright policy)
  • Publisher: American Chemical Society (ACS)
Abstract
The δ-endotoxin family of toxic proteins represents the major component of the insecticidal capability of the bacterium Bacillus thuringiensis. Domain I of the toxins, which is largely α-helical, has been proposed to unfold at protein entry into the membrane of a target insect, following models known as the penknife and umbrella models. We extended the analysis of a previous work in which four disulfide bridges were constructed in domain I of the Cry1Aa δ-endotoxin that putatively prevented unfolding during membrane partitioning. Using bioassays and voltage clamping of whole insect midgut instead of artificial lipid bilayers, it was found that, while toxicity an...
Subjects
Medical Subject Headings: fungi
free text keywords: Biochemistry
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