کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2065197 1076910 2009 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Expression, purification and characterization of the Cry2Aa14 toxin from Bacillus thuringiensis subsp. kenyae
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیوشیمی، ژنتیک و زیست شناسی مولکولی (عمومی)
پیش نمایش صفحه اول مقاله
Expression, purification and characterization of the Cry2Aa14 toxin from Bacillus thuringiensis subsp. kenyae
چکیده انگلیسی

An indigenous strain HD-550 of Bacillus thuringiensis subsp. kenyae was found to be toxic to lepidopteran as well as dipteran insects. The cry2Aa gene (classified as cry2Aa14) from this isolate was cloned and expressed in Escherichia coli. Only a little amount of the expressed Cry2Aa14 protein was observed in soluble fraction under normal induction condition. The inclusions were non-toxic to test insects, whereas solubilized Cry2Aa14 was highly toxic to lepidopteran and dipteran insects. Cry2Aa14 protein was expressed as thioredoxin (trx) fusion protein for improving the yield of active protein. An enhancement of nearly 15% was observed in the yield of active Cry2Aa14. The TrxA–Cry2Aa14 protein purified from the solubilized fraction also showed toxicity profile similar to the wild-type protein. The LC50 values of Cry2Aa14 and TrxA–Cry2Aa14 protein against Spodoptera litura was 694 and 696 ng/cm2, respectively, while for Culex quinquefasciatus the LC50 values were 894 and 902 ng/ml, respectively. The broad spectrum toxicity of the Cry2Aa14 thus indicates that this protein could be an important component in integrated pest management. Further, the trx tag clearly led to higher yield, which facilitates protein purification for biophysical and biochemical characterization.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Toxicon - Volume 54, Issue 4, 15 September 2009, Pages 519–524
نویسندگان
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