Variant cry1Ab entomocidal Bacillus thuringiensis toxin gene facilitates the recovery of an increased number of lepidopteran insect resistant independent rice transformants against yellow stem borer (Scirpophaga incertulus) inflicted damage

The primary technical constraint plant scientists face in generating insect resistant transgenic crops with insecticidal Bacillus thuringiensis (Bt) crystal protein (Cry) genes remains failing to generate sufficiently large numbers of effective resistant transgenic plant lines. One possible means to...

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Bibliographic Details
Published in:Journal of plant biochemistry and biotechnology 2014, Vol.23 (1), p.81-92
Main Authors: Dandapat, Abhijit, Bhattacharyya, Jagannath, Gayen, Srimonta, Chakraborty, Anirban, Banga, Anannya, Mukherjee, Rajeswari, Mandal, Chandi Charan, Hossain, Munshi Azad, Roy, Samarjit, Basu, Asitava, Sen, Soumitra Kumar
Format: Article
Language:English
Subjects:
Bacillus thuringiensis
Biomedical and Life Sciences
Cell Biology
genes
insect pests
Lepidoptera
Life Sciences
Original Article
Oryza sativa
phenylalanine
Plant Biochemistry
Protein Science
Receptors
rice
scientists
Scirpophaga incertulas
serine
spectral analysis
toxicity
transgenic plants
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Summary:The primary technical constraint plant scientists face in generating insect resistant transgenic crops with insecticidal Bacillus thuringiensis (Bt) crystal protein (Cry) genes remains failing to generate sufficiently large numbers of effective resistant transgenic plant lines. One possible means to overcome this challenge is through deployment of a Cry toxin gene that contains high levels of insecticidal specific activity for target insect pests. In the present study, we tested this hypothesis using a natural variant of the Cry1Ab toxin under laboratory conditions that possessed increased insecticidal potency against the yellow stem borer (YSB, Scirpophaga incertulus), one of the most damaging rice insect pests. Following adoption of a stringent selection strategy for YSB resistant transgenic rice lines under field conditions, results showed recovery of a significantly higher number of YSB resistant independent transgenic plant lines with the variant cry1Ab gene relative to transgenic plant lines harbouring cry1Ab berliner gene. Structural homology modelling of the variant toxin peptide with the Cry1Aa toxin molecule, circular dichroism spectral analysis, and hydropathy plot analysis indicated that serine substitution by phenylalanine at amino acid position 223 of the Cry1Ab toxin molecule resulted in a changed role for α-helix 7 in domain I of Cry1Ab for enhanced toxicity.
ISSN:0971-7811
0974-1275
DOI:10.1007/s13562-013-0190-1