Bacillus thuringiensis Cry1Ab Domain III β-16 Is Involved in Binding to Prohibitin, Which Correlates with Toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae)

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Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversidad Nacional Autónoma de Mexico-
Autor(es): dc.contributorChinese Academy of Agricultural Sciences-
Autor(es): dc.creatorSena da Silva, Igor Henrique [UNESP]-
Autor(es): dc.creatorGómez, Isabel-
Autor(es): dc.creatorPacheco, Sabino-
Autor(es): dc.creatorSánchez, Jorge-
Autor(es): dc.creatorZhang, Jie-
Autor(es): dc.creatorLuque Castellane, Tereza Cristina [UNESP]-
Autor(es): dc.creatorAparecida Desiderio, Janete [UNESP]-
Autor(es): dc.creatorSoberón, Mario-
Autor(es): dc.creatorBravo, Alejandra-
Autor(es): dc.creatorPolanczyk, Ricardo Antônio [UNESP]-
Data de aceite: dc.date.accessioned2022-02-22T00:53:05Z-
Data de disponibilização: dc.date.available2022-02-22T00:53:05Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-01-03-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1128/AEM.01930-20-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/208321-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/208321-
Descrição: dc.descriptionHelicoverpa armigera is a major insect pest of several crops worldwide. This insect is susceptible to some Bacillus thuringiensis (Bt) Cry insecticidal proteins expressed in transgenic crops or used in biopesticides. Previously, we identified H. armigera prohibitin (HaPHB) as a Cry1Ac-binding protein. Here, we further analyzed the potential role of PHB as a Cry toxin receptor in comparison to cadherin (CAD), well recognized as a Cry1Ac receptor. HaPHB-2 midgut protein and HaCAD toxin-binding region (TBR) fragment from H. armigera were expressed in Escherichia coli cells, and binding assays with different Cry1 toxins were performed. We demonstrated that Cry1Ab, Cry1Ac, and Cry1Fa toxins bound to HaPHB-2 in a manner similar to that seen with HaCAD-TBR. Different Cry1Ab mutant toxins located in domain II (Cry1AbF371A and Cry1AbG439D) or domain III (Cry1AbL511A and Cry1AbN514A), which were previously characterized and found to be affected in receptor binding, were analyzed regarding their binding interaction with HaPHB-2 and toxicity against H. armigera One β-16 mutant (Cry1AbN514A) showed increased binding to HaPHB-2 that correlated with 6-fold-higher toxicity against H. armigera, whereas the other β-16 mutant (Cry1AbL511A) was affected in binding to HaPHB-2 and lost toxicity against H. armigera Our data indicate that β-16 from domain III of Cry1Ab is involved in interactions with HaPHB-2 and in toxicity. This report identifies a region of Cry1Ab involved in binding to HaPHB-2 from a Lepidoptera insect, suggesting that this protein may participate as a novel receptor in the mechanism of action of the Cry1 toxins in H. armigeraIMPORTANCEHelicoverpa armigera is a polyphagous pest that feeds on important crops worldwide. This insect pest is sensitive to different Cry1 toxins from Bacillus thuringiensis In this study, we analyzed the potential role of PHB-2 as a Cry1 toxin receptor in comparison to CAD. We show that different Cry1 toxins bound to HaPHB-2 and HaCAD-TBR similarly and identify β-16 from domain III of Cry1Ab as a binding region involved in the interaction with HaPHB-2 and in toxicity. This report characterized HaPHB-Cry1 binding interaction, providing novel insights into potential target sites for improving Cry1 toxicity against H. armigera.-
Descrição: dc.descriptionDepartment of Agricultural Production Sciences School of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionDepartment of Molecular Microbiology Instituto de Biotecnología Universidad Nacional Autónoma de Mexico-
Descrição: dc.descriptionState Key Laboratory for Biology of Plant Diseases and Insect Pests Institute of Plant Protection Chinese Academy of Agricultural Sciences-
Descrição: dc.descriptionDepartment of Applied Biology to Farming School of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionDepartment of Agricultural Production Sciences School of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)-
Descrição: dc.descriptionDepartment of Applied Biology to Farming School of Agricultural and Veterinarian Sciences São Paulo State University (Unesp)-
Idioma: dc.languageen-
Relação: dc.relationApplied and environmental microbiology-
???dc.source???: dc.sourceScopus-
Palavras-chave: dc.subjectBacillus thuringiensis-
Palavras-chave: dc.subjectcadherin-
Palavras-chave: dc.subjectCotton bollworm-
Palavras-chave: dc.subjectCry toxins-
Palavras-chave: dc.subjectHelicoverpa armigera-
Palavras-chave: dc.subjectmechanism of action-
Palavras-chave: dc.subjectPHB-
Palavras-chave: dc.subjectprohibitin-
Título: dc.titleBacillus thuringiensis Cry1Ab Domain III β-16 Is Involved in Binding to Prohibitin, Which Correlates with Toxicity against Helicoverpa armigera (Lepidoptera: Noctuidae)-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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