Construction of a Bacillus thuringiensis genetically-engineered strain harbouring the secreted Cry1Ia delta-endotoxin in its crystal

被引:0
作者
Mariam Dammak
Samir Jaoua
Slim Tounsi
机构
[1] University of Sfax,Biopesticides Team, Centre of Biotechnology of Sfax
[2] Qatar University,Biological & Environmental Sciences Department, College of Arts and Sciences
来源
Biotechnology Letters | 2011年 / 33卷
关键词
Cry1Ia; -terminal domain; Co-crystallization; Production; Toxicity;
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摘要
Unlike other Bacillus thuringiensis Cry proteins, Cry1Ia does not form a crystal since it is a secreted delta-endotoxin. We have engineered a Cry1Iac chimeric protein by substituting the C-terminal part of Cry1Ia by the corresponding Cry1Ac part. When expressed in an acrystalliferous B. thuringiensis strain, Cry1Iac did not crystallize, but when expressed in the crystalliferous strain BNS3, the chimeric protein co-crystallized with the endogenous Cry1A delta-endotoxins forming a typical bipyramidal crystal. The integration of Cry1Ia in the composition of the crystal of BNS3 led to an increase of its delta-endotoxin production (13%) and to an improvement (60%) of its toxicity against Agrotis ipsilon.
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页码:2367 / 2372
页数:5
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