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The full-length Cry1Ac protoxin without proteolytic activation exhibits toxicity against insect cell line CF-203
- Source :
- Journal of Invertebrate Pathology. 152:25-29
- Publication Year :
- 2018
- Publisher :
- Elsevier BV, 2018.
-
Abstract
- The new dual model for Bacillus thuringiensis insecticidal mechanism proposed that Cry1A protoxins without proteolytic activation could bind to insect midgut receptors to exert toxicity. To evaluate insecticidal potency of Cry1Ac protoxin at precluding interference of midgut proteases, the cytotoxicity of Cry1Ac protoxin against midgut cell line CF-203 derived from Choristoneura fumiferana was analyzed. It was revealed that Cry1Ac protoxin was toxic to CF-203 cells and there existed certain differences in the cytological changes when treated with protoxin and toxin. Our cell-based study provided direct evidence for the proposed dual model and shed light on exploring the difference between two toxic pathways elicited by intact protoxin and activated toxin.
- Subjects :
- 0301 basic medicine
Proteases
Insecta
Bacillus thuringiensis
medicine.disease_cause
Cell Line
Hemolysin Proteins
03 medical and health sciences
Bacterial Proteins
medicine
Animals
Cytotoxicity
Receptor
Ecology, Evolution, Behavior and Systematics
Bacillus thuringiensis Toxins
030102 biochemistry & molecular biology
biology
Toxin
fungi
Midgut
biology.organism_classification
Endotoxins
030104 developmental biology
Cry1Ac
Biochemistry
Cell culture
Proteolysis
Subjects
Details
- ISSN :
- 00222011
- Volume :
- 152
- Database :
- OpenAIRE
- Journal :
- Journal of Invertebrate Pathology
- Accession number :
- edsair.doi.dedup.....5413029db6723ad33878866b9ca00014
- Full Text :
- https://doi.org/10.1016/j.jip.2018.01.004