V-ATPase Subunit B is a Functional Receptor of Cry1Ac in Helicoverpa armigera (Lepidoptera:Noctuidae)

doi:10.16409/j.cnki.2095-039x.2022.09.005

Abstract

Abstract: Current studies on the mode of action of Bacillus thuringiensis(Bt) have found that vacuolar-type proton ATPase (V-ATPase) may be a new receptor of Bt proteins.In our previous study of screening for Cry1Ac binding protein from the midgut yeast library of cotton bollworm,we found that V-ATPase subunit B (V-ATPase B) was a Cry1Ac binding receptor.To clarify the role of V-ATPase B in Cry1Ac toxicity and insect resistance to Cry1Ac,we measured the expression levels of V-ATPase B in Cry1Ac-susceptible and-resistance strains and in Cry1Ac induced larvae using real-time quantitative PCR (RT-PCR),characterized the binding of V-ATPase B with Cry1Ac protein using Ligand blot,and tested the functions of V-ATPase B in the toxicity of Cry1Ac by expressing V-ATPase B in Sf9 cells.The results showed significantly reduced expression levels of V-ATPase B in Cry1Ac-resistant and Cry1Ac-feeding H.armigera larvae. Ligand blot experiments verified the interaction between V-ATPase B and Cry1Ac protein.Importantly,overexpressing V-ATPase B in cells caused higher cytotoxicity of Cry1Ac.These results suggest that V-ATPase subunit B is a functional receptor of Cry1Ac and may be involved in resistance evolution of cotton bollworm to Cry1Ac through reducing its expression.

Key words: V-ATPase B, Helicoverpa armigera, Cry1Ac, cytotoxicity

CLC Number:

S476.1

DUAN Yunpeng, YAO Xue, LI Pin, WANG Menghan, HU Shouyin, HU Enjing, LIU Yonggang, YANG Shufang, WEI Jizhen. V-ATPase Subunit B is a Functional Receptor of Cry1Ac in Helicoverpa armigera (Lepidoptera:Noctuidae)[J]. Chinese Journal of Biological Control, 2022, 38(5): 1094-1102.

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