Endogenous serpin reduces toxicity of Bacillus thuringiensis Cry1Ac against Helicoverpa armigera (Hubner)

Bt protoxins are required to convert to a smaller activated form by insect midgut proteases to exert toxicity against insect pests. Serine protease inhibitors (serpins) play a valuable part in gut protease of insect that hamper digestive proteases activity of insects. Whether the insect serpins induced by Bt protoxin affect the insecticidal activity were rare studied. Here, we identified a serpin-e gene from Helicoverpa armigera, which had potential RCL (Reactive Center Loop) region near the C-terminus like other serpin proteins. It widely expressed in different development stages and in various tissues, but highest expressed in fourth-instar larvae and in larval hemolymph. This Haserpin-e could be induced by Cry1Ac protoxin in vivo and inhibit the midgut proteases to activate Cry1Ac in vitro. Importantly, the functional study indicated it could inhibit the process from Cry1Ac protoxin to activated toxin, and led to the reduction of Cry1Ac insecticide activity to cotton bollworm. Based on our results, we proposed that Haserpin-e involved in the toxicity of Cry1Ac to cotton bollworm by blocking the serine protease to activate the protoxin.

Automated summary

The study identified a serpin-e gene from Helicoverpa armigera, which is widely expressed and highly expressed in fourth-instar larvae and larval hemolymph. It can be induced by Cry1Ac protoxin and inhibits midgut proteases to activate Cry1Ac, contributing to the reduction of Cry1Ac insecticide activity in cotton bollworm. This suggests that serpin-e is involved in the toxicity of Cry1Ac to cotton bollworm by blocking serine protease activation of the protoxin.