Abstract
Background The use of Bt crystal protein as a natural insecticide, applied directly to crops has been true for many years. Cry genes codifing these proteins are already are being used in transformation plants that become resistant to certain insects. The aim of this study was to compare the amino acid sequences that encode the Cry protein to insects of the orders Lepidoptera, Diptera and Lepidoptera / Diptera. We evaluated 15 sequences that were deposited in the GenBank and using bioinformatics tools to align and compare these sequences that present three domains (I, II, and III). It is assumed that changes in these domain influence the toxicity of the protein and her order. The results presented indicate the presence of specific regions and that may be related to the specificity of protein toxicity.
Highlights
The use of Bt crystal protein as a natural insecticide, applied directly to crops has been true for many years
To compare the sequences based on similarities between the genes that act on a particular species we selected 5 genes described that attack insects of the order Lepidoptera: Cry1Ba1, Cry1Ba2, Cry1Bb1, Cry1Ca1, 1Instituto Federal de Educação, Ciência e Tecnologia do Sul de Minas Campus Machado, Carvalhópolis, Brazil 2Universidade de Ribeirão Preto - Unaerp, Ribeirão Preto, Brazil Full list of author information is available at the end of the article
Position 224 in domain II, and domain III at position 84 was exchanged amino acids increasing the stability of proteins by promoting hydrophobic interactions in the your interior
Summary
The use of Bt crystal protein as a natural insecticide, applied directly to crops has been true for many years. Cry genes codifing these proteins are already are being used in transformation plants that become resistant to certain insects. The aim of this study was to compare the amino acid sequences that encode the Cry protein to insects of the orders Lepidoptera, Diptera and Lepidoptera / Diptera. It is assumed that changes in these domain influence the toxicity of the protein and her order. The results presented indicate the presence of specific regions and that may be related to the specificity of protein toxicity
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