1. Alkaline phosphatase 2 is a functional receptor of Cry1Ac but not Cry2Ab in Helicoverpa zea
- Author
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Xianchun Li, Jizhen Wei, Min Zhang, and G. Liang
- Subjects
0106 biological sciences ,0301 basic medicine ,viruses ,Fat Body ,Bacillus thuringiensis ,Sf9 ,Moths ,Spodoptera ,01 natural sciences ,Cell Line ,Hemolysin Proteins ,03 medical and health sciences ,Bacterial Proteins ,Genetics ,Animals ,Receptor ,Molecular Biology ,Bacillus thuringiensis Toxins ,biology ,Ovary ,fungi ,food and beverages ,RNA ,Alkaline Phosphatase ,biology.organism_classification ,Molecular biology ,Endotoxins ,Gastrointestinal Tract ,010602 entomology ,RNA silencing ,030104 developmental biology ,Cell culture ,Gene Knockdown Techniques ,Larva ,Insect Science ,Insect Proteins ,Alkaline phosphatase ,Female ,Helicoverpa zea - Abstract
Although membrane-bound alkaline phosphatases (ALPs) have been proposed as a receptor for Cry1Ac in a few lepidopteran species, their potential functions as a Cry2Ab receptor are yet to be verified. To determine if ALP2 also serves as a receptor for Cry1Ac and even for Cry2Ab in Helicoverpa zea, we measured the potency of activated Cry1Ac and Cry2Ab against midgut and fat body cell lines of H. zea and the ovarian cell line of Spodoptera frugiperda (Sf9) expressing H. zea ALP2 (HzALP2) or transfected with HzALP2 double-stranded RNA (dsRNA). Relative to the control cells, the three cell lines expressing HzALP2 were more susceptible to Cry1Ac but there was no difference for Cry2Ab. By contrast, the two H. zea cell lines transfected with HzALP2 dsRNA were resistant to Cry1Ac while kept susceptible to Cry2Ab. Furthermore, RNA interference knockdown of HzALP2 in H. zea larvae enhanced larval survival on Cry1Ac-containing diets. These findings indicate that HzALP2 functions as a receptor of Cry1Ac but not Cry2Ab.
- Published
- 2019