Abstract

Bacillus thuringiensis is the most successful microbial insecticide agent and its proteins have been studied for many years due to its toxicity against insects mainly belonging to the orders Lepidoptera, Diptera and Coleoptera, which are pests of agro-forestry and medical-veterinary interest. However, studies on the interactions between this bacterium and the insect species classified in the order Coleoptera are more limited when compared to other insect orders. To date, 45 Cry proteins, 2 Cyt proteins, 11 Vip proteins, and 2 Sip proteins have been reported with activity against coleopteran species. A number of these proteins have been successfully used in some insecticidal formulations and in the construction of transgenic crops to provide protection against main beetle pests. In this review, we provide an update on the activity of Bt toxins against coleopteran insects, as well as specific information about the structure and mode of action of coleopteran Bt proteins.

Highlights

  • The use of entomopathogenic microorganisms as biological control agents has become one of the most effective alternatives to chemical pest control

  • Bacillus thuringiensis (Bt) is the most important entomopathogenic microorganism used to date in crop protection

  • bacteriumBacillus thuringiensis (Bt) synthesizes insecticidal toxins associated with the vegetative growth phase, named vegetative insecticidal proteins (Vip) and secreted insecticidal proteins (Sip), which are secreted into the growth medium [4]

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Summary

Introduction

The use of entomopathogenic microorganisms as biological control agents has become one of the most effective alternatives to chemical pest control. Identity but a structural similarity as high as Phylogenetic analysis the independent evolution of the three structural domains as well as from the swapping of shows domain that the greatdifferent variability in the insecticidal activity of this 3-domain group has resulted from the III between toxins independent evolution of the three structural domains as well as from the damage swapping domain. Due to their feeding habits, many species of coleoptera cause serious to of both cultivated between different toxins plants and stored products, leading to significant economic losses in all regions of the world [17,18]. Cyt proteins are toxic to coleopteran pests and increase the potential of certain Cry toxins [20]. [20]

Protein
Non-3-Domain Cry Toxins
Cyt Proteins
Insecticidal Activity
Host Range
Genetically Engineered Cry Genes
Mode of Action
Solubilization and Proteolytic Processing
Binding to the Larval Epithelium
Oligomerization and Pore Formation
The Secretable Coleopteran-Active Proteins
Protein Structure
Bt Based Insecticides
Bt-Crops
Findings
Resistance and Cross-Resistance

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