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Cry1Ac Protoxin and Its Activated Toxin from Bacillus thuringiensis Act Differentially during the Pathogenic Process
Lingling Qi1, Xianfeng Qiu1, Sisi Yang1
1College of Life Science, State Key Laboratory of Developmental Biology of Freshwater Fish, Hunan Normal University, Changsha 410081, People's Republic of China.
Bacillus thuringiensis (Bt) Cry1A proteins have a dual mode of action. This study reveals distinct molecular pathways and binding sites for Bt Cry1Ac protoxin and activated toxin, clarifying their insecticidal mechanisms.
Area of Science:
- Molecular Biology
- Insect Toxicology
- Biochemistry
Background:
- The dual model of Bacillus thuringiensis (Bt) insecticidal mechanism suggests both Cry1A protoxin and activated toxin kill insects.
- However, molecular-level differences in toxic pathways between protoxin and activated toxin remain unclear.
Purpose of the Study:
- To investigate the molecular differences in toxicity pathways between Cry1Ac protoxin and activated toxin.
- To elucidate the binding sites and endocytosis pathways of Cry1Ac protoxin and activated toxin.
Main Methods:
- Utilized the CF-203 cell line derived from the midgut of Choristoneura fumiferana.
- Analyzed Cry1Ac protoxin presence and binding sites in the midgut of Plutella xylostella.
Main Results:
- Identified distinct binding sites and endocytosis pathways for Cry1Ac protoxin and activated toxin in CF-203 cells.
- Observed predominant Cry1Ac protoxin in Plutella xylostella midgut early after ingestion, causing epithelial damage.
- Demonstrated different binding sites on brush border membrane vesicles for protoxin compared to the activated toxin.
Conclusions:
- Findings support the dual mode of action for Bacillus thuringiensis Cry1A proteins.
- Improved understanding of the molecular features contributing to Cry1Ac protoxin toxicity.
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