title: 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.
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 125(th) 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.
authors.affiliation: Rhizosphere Biology Laboratory, Department of Microbiology, Bharathidasan University, Tiruchirappalli - 620024, TamilNadu, India.
authors.forename: King Solomon
authors.initials: KS
authors.lastname: Ebenezer
authors.forename: Ramesh
authors.initials: R
authors.lastname: Nachimuthu
authors.forename: Prabha
authors.initials: P
authors.lastname: Thiagarajan
authors.forename: Rajesh Kannan
authors.initials: RK
authors.lastname: Velu
keywords: Bacillus thuringiensis; Cross affinity; Crystal protein; Docking; Persistence; Phylogenetic analysis
references.citation: J Anim Sci. 2003 Oct;81(10):2546-51
references.pmid: 14552382
references.citation: Braz J Microbiol. 2011 Jan;42(1):140-6
references.pmid: 24031615
references.citation: Nucleic Acids Res. 2003 Jul 1;31(13):3381-5
references.pmid: 12824332
references.citation: Structure. 2001 May 9;9(5):409-17
references.pmid: 11377201
references.citation: Appl Environ Microbiol. 1996 Aug;62(8):2839-44
references.pmid: 8702276
references.citation: J Mol Biol. 1995 Dec 1;254(3):447-64
references.pmid: 7490762
references.citation: Bioinformation. 2013 May 25;9(9):477-80
references.pmid: 23847403
references.citation: Appl Environ Microbiol. 1995 May;61(5):1786-90
references.pmid: 16535020
references.citation: Toxicol Pathol. 2002 Jan-Feb;30(1):126-8
references.pmid: 11890464
references.citation: J Mol Graph Model. 2012 Mar;33:61-76
references.pmid: 22182469
references.citation: J Mol Biol. 2001 Oct 26;313(3):629-38
references.pmid: 11676544
references.citation: Biol Lett. 2010 Feb 23;6(1):74-7
references.pmid: 19740894
references.citation: EMBO J. 1986 Apr;5(4):823-6
references.pmid: 3709526
references.citation: Proteomics. 2005 Sep;5(14):3696-711
references.pmid: 16167365