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Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hübner)
Author(s) -
Wang Bingjie,
Wei Jizhen,
Wang Yanan,
Chen Lin,
Liang Gemei
Publication year - 2020
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.21661
Subject(s) - cry1ac , helicoverpa armigera , biology , lepidoptera genitalia , toxin , botany , gene , genetically modified crops , microbiology and biotechnology , biochemistry , transgene
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 ( K d = 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.