V-ATPase C Acts as a Receptor for <i>Bacillus thuringiensis</i> Cry2Ab and Enhances Cry2Ab Toxicity to <i>Helicoverpa armigera</i>

V-ATPase C Acts as a Receptor for <i>Bacillus thuringiensis</i> Cry2Ab and Enhances Cry2Ab Toxicity to <i>Helicoverpa armigera</i>

Cry2Ab is a significant alternative <i>Bacillus thuringiensis</i> (<i>Bt</i>) protein utilized for managing insect resistance to Cry1 toxins and broadening the insecticidal spectrum of crops containing two or more <i>Bt</i> genes. Unfortunately, the identified rec...

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Bibliographic Details
Main Authors: Pin Li, Yuge Zhao, Ningbo Zhang, Xue Yao, Xianchun Li, Mengfang Du, Jizhen Wei, Shiheng An
Format: Article
Language:English
Published: MDPI AG 2024-11-01
Series:Insects
Subjects:
<i>Bacillus thuringiensis</i>
<i>Helicoverpa armigera</i>
V-ATPase C
Cry2Ab
binding
toxicity
Online Access:https://www.mdpi.com/2075-4450/15/11/895
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Summary:Cry2Ab is a significant alternative <i>Bacillus thuringiensis</i> (<i>Bt</i>) protein utilized for managing insect resistance to Cry1 toxins and broadening the insecticidal spectrum of crops containing two or more <i>Bt</i> genes. Unfortunately, the identified receptors fail to fully elucidate the mechanism of action underlying Cry2Ab. Previous studies have demonstrated the involvement of vacuolar H<sup>+</sup>-ATPase subunits A, B, and E (V-ATPase A, B, and E) in <i>Bt</i> insecticidal activities. The present study aims to investigate the contribution of V-ATPase C to the toxicities of Cry2Ab against <i>Helicoverpa armigera</i>. The feeding of Cry2Ab in <i>H. armigera</i> larvae resulted in a significant decrease in the expression of V-ATPase C. Further investigations confirmed the interaction between V-ATPase C and activated Cry2Ab protein according to Ligand blot and homologous and heterologous competition assays. Expressing endogenous <i>HaV-ATPase C</i> in Sf9 cells resulted in an increase in Cry2Ab cytotoxicity, while the knockdown of V-ATPase C by double-stranded RNAs (dsRNA) in midgut cells decreased Cry2Ab cytotoxicity. Importantly, a higher toxicity of the mixture containing Cry2Ab and V-ATPase C against insects was also observed. These findings demonstrate that V-ATPase C acts as a binding receptor for Cry2Ab and is involved in its toxicity to <i>H. armigera</i>. Furthermore, the synergy between V-ATPase C protein and Cry2Ab protoxins provides a potential strategy for enhancing Cry2Ab toxicity or managing insect resistance.
ISSN:2075-4450

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