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The β-type anti-Id (Ab2β) is considered to have potential for simulating the structure and function of the antigen. In this study, a β-type anti-Id (3A7 anti-I-GEAb) of the Cry1C toxin was captured from a GEAb library. Subsequently, a higher activity of mutant (3A7 mutant 8) was obtained from the mutagenesis library based on 3A7 anti-I-GEAb. The LD values of 3A7 anti-I-GEAb and 3A7 mutant 8 reach up to 38.9% and 46.8% of Cry1C toxin for and reach up to 32.9% and 37.4% of Cry1C toxin for . Additionally, an IC-ELISA was established based on 3A7 mutant 8 (as the coated "antigen"), with an LOD value of 0.35 ng/mL, exhibiting good accuracy and stability for detecting Cry1C toxin in spiked samples. The present β-type anti-I-GEAb not only exhibits insecticidal activity similar to Cry1C toxin, offering potential for environmentally friendly pest management, but it can also replace the Cry1C toxin structure to establish a highly sensitive and specific IC-ELISA for monitoring Cry1C toxin.
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http://dx.doi.org/10.1021/acs.jafc.4c06376 | DOI Listing |
Sci Rep
July 2025
Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 West Yuanmingyuan Road, Haidian District, Beijing, 100193, People's Republic of China.
Fish is an excellent model animal with which to assess the potential effects of exogenous toxins. In fields of transgenic Bacillus thuringiensis (Bt) rice, fish would be exposed to Bt protein released from Bt rice into the water environment or by way of direct feeding on deposited plant material. Whether Bt rice pose potential risks to the growth and health of fish have gradually become a focus of attention for environmentalists and the fish farming industry.
View Article and Find Full Text PDFJ Agric Food Chem
October 2024
Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
The β-type anti-Id (Ab2β) is considered to have potential for simulating the structure and function of the antigen. In this study, a β-type anti-Id (3A7 anti-I-GEAb) of the Cry1C toxin was captured from a GEAb library. Subsequently, a higher activity of mutant (3A7 mutant 8) was obtained from the mutagenesis library based on 3A7 anti-I-GEAb.
View Article and Find Full Text PDFJ Agric Food Chem
September 2024
State Key Laboratory Cultivation Base, Ministry of Science and Technology─Jiangsu Key Laboratory for Food Quality and Safety, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China.
Synergistic factors can enhance the toxicity of Bt toxins and delay the development of Bt resistance. Previous research has demonstrated that a cadherin fragment (HaCad-TBR) increased the toxicity of Cry1Ac in larvae but did not have a synergistic effect on Cry1B, Cry1C, and Cry1F toxins. In this study, a fusion protein (HaCad-TBR-2D3 V) derived from HaCad-TBR and a Bt Cry1-specific antibody peptide was expressed in .
View Article and Find Full Text PDFGene
November 2024
Rice Research Institute, Heilongjiang Academy of Agricultural Sciences, Jiamusi 154026, China.
Background: Transgenic insect-resistant rice offers an environmentally friendly approach to mitigate yield losses caused by lepidopteran pests, such as stem borers. Bt (Bacillus thuringiensis) genes encode insecticidal proteins and are widely used to confer insect resistance to genetically modified crops. This study investigated the integration, inheritance, and expression characteristics of codon-optimised synthetic Bt genes, cry1C* and cry2A*, in transgenic early japonica rice lines.
View Article and Find Full Text PDFAnal Biochem
October 2024
Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Institute of Food Safety and Nutrition, Jiangsu Academy of Agricultural Sciences, Nanjing, 210014, China; School of Food and Biological Engineering, Jiangsu University, Zhe
Using the amino acid sequences and analysis of selected known structures of Bt Cry toxins, Cry1Ab, Cry1Ac, Cry1Ah, Cry1B, Cry1C and Cry1F we specifically designed immunogens. After antibodies selection, broad-spectrum polyclonal antibodies (pAbs) and monoclonal antibody (namely 1A0-mAb) were obtained from rabbit and mouse, respectively. The produced pAbs displayed broad spectrum activity by recognizing Cry1 toxin, Cry2Aa, Cry2Ab and Cry3Aa with half maximal inhibitory concentration (IC) values of 0.
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