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Activation of Bacillus thuringiensis Cry1I to a 50 kDa stable core impairs its full toxicity to Ostrinia nubilalis

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Activation of Bacillus thuringiensis Cry1I to a 50 kDa stable core impairs its full toxicity to Ostrinia nubilalis

dc.contributor.author	Khorramnejad, Ayda
dc.contributor.author	Bel Cortés, Yolanda
dc.contributor.author	Talaei‑Hassanloui, Reza
dc.contributor.author	Escriche Soler, Baltasar
dc.date.accessioned	2023-05-17T16:36:03Z
dc.date.available	2023-05-17T16:36:03Z
dc.date.issued	2022
dc.identifier.citation	Khorramnejad, Ayda Bel Cortés, Yolanda Talaei&#8209Hassanloui, Reza Escriche Soler, Baltasar 2022 Activation of Bacillus thuringiensis Cry1I to a 50 kDa stable core impairs its full toxicity to Ostrinia nubilalis Applied Microbiology and Biotechnology 106 1745 1758
dc.identifier.uri	https://hdl.handle.net/10550/86688
dc.description.abstract	Bacillus thuringiensis Cry1I insecticidal proteins are structurally similar to other three-domain Cry proteins, although their size, activity spectrum, and expression at the stationary phase are unique among other members of the Cry1 family. The mode of action of Cry1 proteins is not completely understood but the existence of an activation step prior to specific binding is widely accepted. In this study, we attempted to characterize and determine the importance of the activation process in the mode of action of Cry1I, as Cry1Ia protoxin or its partially processed form showed significantly higher toxicity to Ostrinia nubilalis than the fully processed protein either activated with trypsin or with O. nubilalis midgut juice. Oligomerization studies showed that Cry1Ia protoxin, in solution, formed dimers spontaneously, and the incubation of Cry1Ia protoxin with O. nubilalis brush border membrane vesicles (BBMV) promoted the formation of dimers of the partially processed form. While no oligomerization of fully activated proteins after incubation with BBMV was detected. The results of the in vitro competition assays showed that both the Cry1Ia protoxin and the approx. 50 kDa activated proteins bind specifically to the O. nubilalis BBMV and compete for the same binding sites. Accordingly, the in vivo binding competition assays show a decrease in toxicity following the addition of an excess of 50 kDa activated protein. Consequently, as full activation of Cry1I protein diminishes its toxicity against lepidopterans, preventing or decelerating proteolysis might increase the efficacy of this protein in Bt-based products.
dc.language.iso	eng
dc.relation.ispartof	Applied Microbiology and Biotechnology, 2022, num. 106, p. 1745-1758
dc.subject	Proteïnes
dc.subject	Insecticides
dc.title	Activation of Bacillus thuringiensis Cry1I to a 50 kDa stable core impairs its full toxicity to Ostrinia nubilalis
dc.type	journal article
dc.date.updated	2023-05-17T16:36:03Z
dc.identifier.doi	10.1007/s00253-022-11808-2
dc.identifier.idgrec	150988
dc.rights.accessRights	open access