Journal
FEMS MICROBIOLOGY LETTERS
Volume 266, Issue 2, Pages 163-169Publisher
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2006.00527.x
Keywords
Aedes aegypti; Cry11Aa; Cry4Aa; Cry4Ba; receptor binding; processing
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This work shows in vitro processing of Bacillus thuringiensis svar. isralensis Cry toxins and the capacity of the active fragments to bind the midgut microvilli of Aedes aegypti larvae. Processing of Cry11Aa, Cry4Aa and Cry4Ba yielded double fragments of 38-30, 45-20 and 45-18 kDa, respectively. Competition assays showed that all active I-125-Cry toxins are able to specifically bind to brush border membrane fractions and they might share a common class of binding sites. The values of IC50 suggested that toxins do not display high affinity for the receptors from brush border membrane fractions, while dissociation assays showed that binding was irreversible, indicating the insertion of toxins in the cell membrane.
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