2008•Unpublished venueRequires access

Relationships between Aminopeptidase N (APN) and Bt resistance of Lepidoptera

Shaoping Zhang

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Abstract

The use of Cry toxins from Bacillus thuringiensis(Bt) to control insect pests is a revolutionary progress in crop production.Change in binding ability between Bt insecticidal proteins and its receptors may be the main mechanism of Lepidoptera insect resistance to Bt toxin.Aminopeptidase N(APN) is one kind of receptors for Bacillus thuringiensis(Bt) toxin in insect midguts.Through discussing its binding capability with Bt toxin,this paper summarizes the molecular biology mechanism of APN gene and Bt resistance of Lepidoptera,and introduces a new model for the mode of Cry1Ac toxin action.

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What this paper is about

The use of Cry toxins from Bacillus thuringiensis(Bt) to control insect pests is a revolutionary progress in crop production.Change in binding ability between Bt insecticidal proteins and its receptors may be the main mechanism of Lepidoptera insect resistance to Bt toxin.Aminopeptidase N(APN) is one kind of receptors for Bacillus thuringiensis(Bt) toxin in insect midguts.Through discussing its binding capability with Bt toxin,this paper summarizes the molecular biology mechanism of APN gene and Bt resistance of Lepidoptera,and introduces a new model for the mode of Cry1Ac toxin action.

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Available abstract

The use of Cry toxins from Bacillus thuringiensis(Bt) to control insect pests is a revolutionary progress in crop production.Change in binding ability between Bt insecticidal proteins and its receptors may be the main mechanism of Lepidoptera insect resistance to Bt toxin.Aminopeptidase N(APN) is one kind of receptors for Bacillus thuringiensis(Bt) toxin in insect midguts.Through discussing its binding capability with Bt toxin,this paper summarizes the molecular biology mechanism of APN gene and Bt resistance of Lepidoptera,and introduces a new model for the mode of Cry1Ac toxin action.

Key concepts: Bacillus thuringiensis, Cry1Ac, Lepidoptera genitalia, Biology, Toxin, Insect, Aminopeptidase, Crop

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