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Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hübner)
- Source :
- Archives of insect biochemistry and physiologyREFERENCES. 104(1)
- Publication Year :
- 2019
-
Abstract
- Polycalin has been confirmed as a binding protein of the Cry toxins in a few Lepidoptera insects, but its function in the action mechanism of Cry1Ac and whether it is involved in resistance evolution are still unclear. In this study, Ligand blot and enzyme-linked immunosorbent assays showed that Helicoverpa armigera polycalin could specifically interact with Cry1Ac with a high affinity (Kd = 118.80 nM). Importantly, antisera blocking polycalin in H. armigera larvae decreased the toxicity of Cry1Ac by 31.84%. Furthermore, the relative gene and protein expressions were lower in Cry1Ac-resistant strain (LF60) than that in Cry1Ac-susceptible strain (LF). These findings indicated that H. armigera polycalin was a possible receptor of Cry1Ac and may be contributed to the resistance to Cry1Ac.
- Subjects :
- 0106 biological sciences
0301 basic medicine
Insecticides
Physiology
Helicoverpa armigera
Moths
medicine.disease_cause
01 natural sciences
Biochemistry
Microbiology
Lepidoptera genitalia
Insecticide Resistance
03 medical and health sciences
Hemolysin Proteins
Bacterial Proteins
medicine
Animals
biology
Toxin
Binding protein
fungi
General Medicine
biology.organism_classification
Ligand (biochemistry)
Lipocalins
Blot
Endotoxins
010602 entomology
030104 developmental biology
Cry1Ac
Insect Science
Toxicity
Insect Proteins
Subjects
Details
- ISSN :
- 15206327
- Volume :
- 104
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Archives of insect biochemistry and physiologyREFERENCES
- Accession number :
- edsair.doi.dedup.....73822ce80ce7fec5839eeee9311054e0