Polycalin is involved in the toxicity and resistance to Cry1Ac toxin in Helicoverpa armigera (Hübner). Issue 1 (3rd February 2020)

• Record Type: Journal Article
• Authors: Wang, Bingjie; Wei, Jizhen; Wang, Yanan; Chen, Lin; Liang, Gemei
• Is Part Of: Archives of insect biochemistry and physiology. Volume 104:Issue 1(2020)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2020-02-03
• Subjects: functional receptor -- Helicoverpa armigera -- polycalin -- resistance mechanisms; Insects -- Physiology -- Periodicals; Insect biochemistry -- Periodicals; 595.701572
• DOI: 10.1002/arch.21661
• Languages: English
• ISSNs: 0739-4462

Abstract

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 ( 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. Abstract : Polycalin is involved in the toxicity and resistance to Cry1Ac Research Highlights: Helicoverpa armigera polycalin could specifically bind to the Cry1Ac. The polycalin antisera could reduce the toxicity of Cry1Ac. In the LF60, the relative expression of polycalin reduced both at the transcript and protein level, compared with LF.