Abstract

Bacillus thuringiensis (Bt) is a Gram negative soil bacterium. This bacterium secretes various proteins during different growth phases with an insecticidal potential against many economically important crop pests. One of the important families of Bt proteins is vegetative insecticidal proteins (Vip), which are secreted into the growth medium during vegetative growth. There are three subfamilies of Vip proteins. Vip1 and Vip2 heterodimer toxins have an insecticidal activity against many Coleopteran and Hemipteran pests. Vip3, the most extensively studied family of Vip toxins, is effective against Lepidopteron. Vip proteins do not share homology in sequence and binding sites with Cry proteins, but share similarities at some points in their mechanism of action. Vip3 proteins are expressed as pyramids alongside Cry proteins in crops like maize and cotton, so as to control resistant pests and delay the evolution of resistance. Biotechnological- and in silico-based analyses are promising for the generation of mutant Vip proteins with an enhanced insecticidal activity and broader spectrum of target insects.

Highlights

  • Common soil bacterium Bacillus thuringiensis (Bt) is a Gram positive motile bacterium that gained significant popularity over the past decades because of its role as an invertebrate pest killer [1].B. thuringiensis has been extensively studied for its ability to produce immense arsenal of toxins with an insecticidal potential against insect vectors of human diseases, agricultural pests, nematodes, fungi, gastropods, and protozoans [1,2,3,4,5]

  • vegetative insecticidal proteins (Vip) proteinaceous toxins were isolated from the culture medium of both Bascillus insecticidal proteins (Vip) and secreted insecticidal proteins (Sip), secreted as soluble proteins in a cereus and B. thuringiensis after screening [10,11]

  • Vip proteinaceous toxins were isolated from the culture medium of both Bascillus subfamilies, namely Vip1, Vip2, Vip3, and Vip4, based on their amino acid similarity, which cereus and B. thuringiensis after screening [10,11]

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Summary

Introduction

Common soil bacterium Bacillus thuringiensis (Bt) is a Gram positive motile bacterium that gained significant popularity over the past decades because of its role as an invertebrate pest killer [1]. Vip proteinaceous toxins were isolated from the culture medium of both Bascillus insecticidal proteins (Vip) and secreted insecticidal proteins (Sip), secreted as soluble proteins in a cereus and B. thuringiensis after screening [10,11]. Vip proteinaceous toxins were isolated from the culture medium of both Bascillus subfamilies, namely Vip, Vip, Vip, and Vip, based on their amino acid similarity, which cereus and B. thuringiensis after screening [10,11]. The largest family, Vip, is effective against many species of of Lepidoptera, and crops like cotton and maize have been successfully transformed with various. Vip proteins have no sequence homology with Cry proteins, and do not share not share common binding sites in target insects [16,17,18,19]. 95% similarity, respectively; and the quaternary rank is given with more than 95% identical proteins

Structure and Function of Vip Toxins
Structure and Function of Vip3 Proteins
Vip4 Toxins
Modern Classification of Vip Proteins
Mechanism of Action
Mechanism of Action of Vip3 Toxin
Schematic
Insecticidal
Evolution of Resistance and Cross Resistance to Vip3 Toxins
Identification of Bt Isolates Containing Vip Genes
Transgenic Crops Expressing Vip Proteins
10. In Silico Analyses for Generation of Mutagenic Vip3 Proteins
11. Synergism and Antagonism in Vip3 and Cry Proteins
Findings
12. Future Perspectives
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