Abstract

Bacillus thuringiensis insecticidal proteins (Bt ICPs) are reliable and valuable options for pest management in crops. Protein engineering of Bt ICPs is a competitive alternative for resistance management in insects. The primary focus of the study was to reiterate the translational utility of a protein-engineered chimeric Cry toxin, Cry1AcF, for its broad spectrum insecticidal efficacy using molecular modeling and docking studies. In-depth bioinformatic analysis was undertaken for structure prediction of the Cry toxin as the ligand and aminopeptidase1 receptors (APN1) from Helicoverpa armigera (HaAPN1) and Spodoptera litura (SlAPN1) as receptors, followed by interaction studies using protein-protein docking tools. The study revealed feasible interactions between the toxin and the two receptors through H-bonding and hydrophobic interactions. Further, molecular dynamics simulations substantiated the stability of the interactions, proving the broad spectrum efficacy of Cry1AcF in controlling H. armigera and S. litura. These findings justify the utility of protein-engineered toxins in pest management.

Highlights

  • Battling insects for a better tomorrow is the need of the hour

  • Transgenic technology has emerged as a promising option to help farmers mitigate insect pressure on crops, the most competent option being the use of Bacillus thuringiensis (Bt) insecticidal proteins (ICPs)

  • The global adoption of genetically engineered (GE) crop technology continues at unassuming rates since its introduction

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Summary

Introduction

Battling insects for a better tomorrow is the need of the hour. Transgenic technology has emerged as a promising option to help farmers mitigate insect pressure on crops, the most competent option being the use of Bacillus thuringiensis (Bt) insecticidal proteins (ICPs). The major emphasis of this study was to justify the utility of cry1AcF gene against two pests, and more emphatically to demonstrate the ability of the chimeric toxin to bind and interact with APN1s from both H. armigera and S. litura by exploiting in silico modeling and molecular interactions. This understanding would aid in the development of a stable platform to explain the broad spectrum efficacy of chimeric toxins developed through protein engineering and their use in crop improvement programs

Results and Discussion
Molecular Modeling and Validation
Structure predictionand andvalidation validationof ofaminopeptidase1
Docking and Interaction Analysis
Molecular interaction between and
Molecular Dynamic Simulations
Source of Sequence and Primary Analysis
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