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

Author:

Sena da Silva Igor Henrique1,Gómez Isabel2,Pacheco Sabino2,Sánchez Jorge2,Zhang Jie3,Luque Castellane Tereza Cristina4,Aparecida Desiderio Janete4,Soberón Mario2,Bravo Alejandra2ORCID,Polanczyk Ricardo Antônio1

Affiliation:

1. Department of Agricultural Production Sciences, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil

2. Department of Molecular Microbiology, Instituto de Biotecnología, Universidad Nacional Autónoma de Mexico, Cuernavaca, Morelos, Mexico

3. State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China

4. Department of Applied Biology to Farming, School of Agricultural and Veterinarian Sciences, São Paulo State University (Unesp), Jaboticabal, São Paulo, Brazil

Abstract

Helicoverpa 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 .

Funder

Consejo Nacional de Ciencia y Tecnología

Fundação de Amparo à Pesquisa do Estado de São Paulo

UNAM | Dirección General de Asuntos del Personal Académico, Universidad Nacional Autónoma de México

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

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