in silico identification of cross affinity towards Cry1Ac pesticidal protein with receptor enzyme in Bos taurus and sequence,structure analysis of crystal proteins for stability |
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Authors: | King Solomon Ebenezer Ramesh Nachimuthu Prabha Thiagarajan Rajesh Kannan Velu |
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Institution: | 1.Rhizosphere Biology Laboratory, Department of Microbiology, Bharathidasan University, Tiruchirappalli - 620024, TamilNadu, India;2.School of Biosciences and Technology, Vellore Institute of Technology, Vellore-632014, TamilNadu, India;3.Department of Microbiology, JJ College of Arts and Science, Pudukkottai - 622422, TamilNadu, India |
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Abstract: | Any novel protein introduced into the GM crops need to be evaluated for cross affinity on living organisms. Many researchers are
currently focusing on the impact of Bacillus thuringiensis cotton on soil and microbial diversity by field experiments. In spite of this,
in silico approach might be helpful to elucidate the impact of cry genes. The crystal a protein which was produced by Bt at the time
of sporulation has been used as a biological pesticide to target the insectivorous pests like Cry1Ac for Helicoverpa armigera and
Cry2Ab for Spodoptera sp. and Heliothis sp. Here, we present the comprehensive in silico analysis of Cry1Ac and Cry2Ab proteins
with available in silico tools, databases and docking servers. Molecular docking of Cry1Ac with procarboxypeptidase from
Helicoverpa armigera and Cry1Ac with Leucine aminopeptidase from Bos taurus has showed the 125th amino acid position to be the
preference site of Cry1Ac protein. The structures were compared with each other and it showed 5% of similarity. The cross affinity
of this toxin that have confirmed the earlier reports of ill effects of Bt cotton consumed by cattle. |
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Keywords: | Bacillus thuringiensis Crystal protein Docking Phylogenetic analysis Persistence Cross affinity |
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