Insects, Vol. 15, Pages 895: V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera

Insects, Vol. 15, Pages 895: V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera

Insects doi: 10.3390/insects15110895

Authors: Pin Li Yuge Zhao Ningbo Zhang Xue Yao Xianchun Li Mengfang Du Jizhen Wei Shiheng An

Cry2Ab is a significant alternative Bacillus thuringiensis (Bt) protein utilized for managing insect resistance to Cry1 toxins and broadening the insecticidal spectrum of crops containing two or more Bt genes. Unfortunately, the identified receptors fail to fully elucidate the mechanism of action underlying Cry2Ab. Previous studies have demonstrated the involvement of vacuolar H+-ATPase subunits A, B, and E (V-ATPase A, B, and E) in Bt insecticidal activities. The present study aims to investigate the contribution of V-ATPase C to the toxicities of Cry2Ab against Helicoverpa armigera. The feeding of Cry2Ab in H. armigera 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 HaV-ATPase C 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 H. armigera. Furthermore, the synergy between V-ATPase C protein and Cry2Ab protoxins provides a potential strategy for enhancing Cry2Ab toxicity or managing insect resistance.