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

Overview

Journal Appl Environ Microbiol

Specialties Environmental Health
Microbiology

Date 2020 Oct 31

PMID 33127814

Citations 2

Authors

Igor Henrique Sena da Silva

Isabel Gomez

Sabino Pacheco

Jorge Sanchez

Jie Zhang

Tereza Cristina Luque Castellane

Janete Aparecida Desiderio

Mario Soberon

Alejandra Bravo

Ricardo Antonio Polanczyk

Affiliations

Soon will be listed here.

Abstract

is a major insect pest of several crops worldwide. This insect is susceptible to some (Bt) Cry insecticidal proteins expressed in transgenic crops or used in biopesticides. Previously, we identified 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 were expressed in 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 One β-16 mutant (Cry1AbN514A) showed increased binding to HaPHB-2 that correlated with 6-fold-higher toxicity against , whereas the other β-16 mutant (Cry1AbL511A) was affected in binding to HaPHB-2 and lost toxicity against 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 is a polyphagous pest that feeds on important crops worldwide. This insect pest is sensitive to different Cry1 toxins from 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 .

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