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Recombinant Cry1Ia protein is highly toxic to cotton boll weevil ( Anthonomus grandis Boheman ) and fall armyworm ( Spodoptera frugiperda)
Author(s) -
Martins É.S.,
Aguiar R.W.d.S.,
Martins N.F.,
Melatti V.M.,
Falcão R.,
Gomes A.C.M.M.,
Ribeiro B.M.,
Monnerat R.G.
Publication year - 2008
Publication title -
journal of applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 1364-5072
DOI - 10.1111/j.1365-2672.2007.03665.x
Subject(s) - anthonomus , spodoptera , biology , bacillus thuringiensis , fall armyworm , midgut , bioassay , autographa californica , toxin , sf9 , recombinant dna , biopesticide , botany , gene , microbiology and biotechnology , boll weevil , larva , biochemistry , genetics , bacteria , pesticide , agronomy
Aims: To evaluate the activity of cry1Ia gene against cotton pests, Spodoptera frugiperda and Anthonomus grandis . Methods and Results: Had isolated and characterized a toxin gene from the Bacillus thuringiensis S1451 strain which have been previously shown to be toxic to S. frugiperda and A. grandis . The toxin gene ( cry1Ia ) was amplified by PCR, sequenced, and cloned into the genome of a baculovirus. The Cry1Ia protein was expressed in baculovirus infected insect cells, producing protein inclusions in infected cells. The Cry1Ia protein has used in bioassays against to S. frugiperda and A. grandis. Conclusions: Bioassays using the purified recombinant protein showed high toxicity to S. frugiperda and A. grandis larvae. Molecular modelling of the Cry1Ia protein translated from the DNA sequence obtained in this work, showed that this protein possibly posses a similar structure to the Cry3A protein. Ultrastructural analysis of midgut cells from A. grandis incubated with the Cry1Ia toxin, showed loss of microvilli integrity. Significance and Impact of the Study: The results indicate that the cry1Ia is a good candidate for the construction of transgenic plants resistant to these important cotton pests.