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Polycalin is involved in the action mechanism of Cry2Aa toxin in Helicoverpa armigera (Hübner)
- Source :
- Journal of Integrative Agriculture, Vol 18, Iss 3, Pp 627-635 (2019)
- Publication Year :
- 2019
- Publisher :
- Elsevier, 2019.
-
Abstract
- Receptor proteins on the brush border membrane of the insect midgut epithelium are involved in the mode of action of insecticidal Cry proteins from Bacillus thuringiensis (Bt). Polycalin has been identified as a binding protein of the Bt Cry1Ac toxin in several Lepidoptera including Helicoverpa armigera, but its role in the action mechanism of Cry2Aa is still unclear. In this study, we investigated the binding characteristics of polycalin from the midgut of H. armigera with Cry2Aa and its role in the toxicity of Cry2Aa. The results demonstrated that heterologously expressed H. armigera polycalin peptide could bind with Cry2Aa with high affinity (Kd=32 nmol L–1). The toxicity of Cry2Aa decreased by 27% after H. armigera larvae ingested polycalin antisera. These results suggested that polycalin could be a potential functional receptor for Cry2Aa, and it plays an important role in the susceptibility of H. armigera to Cry2Aa.
- Subjects :
- 0106 biological sciences
Brush border
Agriculture (General)
Plant Science
Helicoverpa armigera
medicine.disease_cause
antisera
01 natural sciences
Biochemistry
S1-972
Food Animals
Bacillus thuringiensis
binding affinity
medicine
Receptor
Ecology
biology
Toxin
Binding protein
fungi
Midgut
04 agricultural and veterinary sciences
biology.organism_classification
Cry1Ac
040103 agronomy & agriculture
0401 agriculture, forestry, and fisheries
Animal Science and Zoology
insecticidal toxicity
polycalin
Agronomy and Crop Science
010606 plant biology & botany
Food Science
Subjects
Details
- Language :
- English
- ISSN :
- 20953119
- Volume :
- 18
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Journal of Integrative Agriculture
- Accession number :
- edsair.doi.dedup.....45e6970e355c711a7f4145ff7f9f4de0