AXMI477 Toxin Variants for Multi-Pest Control and Resistance Management

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Solution Overview

Problem

The intensive use of Bacillus thuringiensis-based insecticides has led to resistance in field populations of certain pests, and modifying pesticidal protein domains can improve control of one pest while potentially reducing resistance to another, necessitating the discovery of new forms of pesticidal toxins that maintain efficacy against multiple target pests.

Innovation Solution

Development of novel recombinant and chimeric nucleic acid molecules encoding pesticidal proteins, such as Axmi477 variants, which confer enhanced resistance to Helicoverpa species while maintaining effectiveness against Plutella xylostella and other pests by altering specific amino acid sequences and domains.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If chemical pesticides are used to control insect pests, then pest control effectiveness is improved, but harmful effects on beneficial insects and development of resistant pest populations occur

Engineering Contradiction:

Improvepest control effectivenessVSAvoidharm to beneficial insects and pest resistance

Core Design Contradiction:

ReliabilityVSObject-affected harmful factors

Solution Approach 1:

The patent applies parameter changes by modifying amino acid residues at positions 198 and 201 in the Cry1C protein sequence to create variants with enhanced activity against Helicoverpa species while maintaining activity against other pests. This specific parameter modification (amino acid substitution) resolves the contradiction by improving target pest control without requiring broader-spectrum chemical pesticides that harm beneficial insects

Inventive Principle:

Principle #35Parameter changes

Solution Approach 2:

The patent creates pesticidal proteins with multi-functionality that can control multiple pest species simultaneously. The modified Cry1C variants maintain activity against original target pests while gaining enhanced activity against Helicoverpa species, reducing the need to use multiple different chemical pesticides and thereby protecting beneficial insects

Inventive Principle:

Principle #6Universality (Multi-functionality)

2Object-affected harmful factors

If B. thuringiensis toxins are used to control pests, then environmental acceptability is improved, but activity against certain pest species like Helicoverpa is insufficient

Engineering Contradiction:

Improveenvironmental acceptabilityVSAvoidpest control activity

Core Design Contradiction:

Object-affected harmful factorsVSReliability

Solution Approach 1:

The patent modifies physical-chemical parameters of the Cry1C protein by substituting amino acids at positions 198 and 201, which enhances the toxin's binding affinity or mechanism of action against Helicoverpa species while preserving the environmentally benign characteristics of B. thuringiensis-derived proteins

Inventive Principle:

Principle #35Parameter changes

Solution Approach 2:

The patent creates composite pesticidal proteins by combining the Cry1C base structure with specific amino acid modifications, resulting in a hybrid toxin that merges the environmental safety of natural B. thuringiensis proteins with enhanced efficacy against previously resistant pest species

Inventive Principle:

Principle #40Composite materials

3Stability of the object's composition

If existing Cry1C protein is used, then activity against original target pests is maintained, but enhanced activity against Helicoverpa species is not achieved

Engineering Contradiction:

Improveactivity against original pestsVSAvoidactivity against Helicoverpa species

Core Design Contradiction:

Stability of the object's compositionVSReliability

Solution Approach 1:

The patent applies local quality changes by making specific amino acid substitutions at positions 198 and 201 in the Cry1C protein. These localized modifications confer enhanced activity against Helicoverpa species while the rest of the protein structure remains unchanged, preserving activity against original target pests

Inventive Principle:

Principle #3Local quality

Applied Scientific Principles

This section explains which scientific principles are used to turn an abstract innovation direction into a practical engineering solution.

Function Achieved in This Case

The Axmi477 variants demonstrate increased resistance to Helicoverpa species and maintain resistance to other pests, providing improved pest control with enhanced efficacy against Lepidopteran, Hemipteran, Coleopteran, and Dipteran pests.

Implementation Method 1

This toxin binds to apical brush border receptors in the midgut of the target larvae and inserts into the apical membrane creating ion channels or pores, resulting in larval death

Methodology Applied

Scientific EffectIon channel formation:

Data Source

PatentUS12630837B2AXMI477 toxin variants and methods for its use

Publication Date: 2026.05.19 BASF CORPORATON

AI summary

Compositions and methods for conferring pesticidal activity to bacteria, plants, plant cells, tissues and seeds are provided. Compositions comprising a coding sequence for a toxin polypeptide are provided. The coding sequences can be used in DNA constructs or expression cassettes for transformation and expression in plants and bacteria. Compositions also comprise transformed bacteria, plants, plant cells, tissues, and seeds. In particular, isolated toxin nucleic acid molecules are provided. Additionally, amino acid sequences corresponding to the polynucleotides are encompassed, and antibodies specifically binding to those amino acid sequences. In particular, the present invention provides for isolated nucleic acid molecules comprising nucleotide sequences encoding the amino acid sequence shown in any of SEQ ID NO: 22 to 42, or the nucleotide sequence set forth in any of SEQ ID NO: 1 to 21, as well as variants and fragments thereof.