Modified Vip3 Polypeptides With CBMs Against Resistant Fall Armyworms
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Solution Overview
Problem
Current Vip3 proteins are limited in their spectrum of insecticidal activity, particularly against Vip3-resistant fall armyworms, and there is a need for alternative insecticidal agents that provide broader protection against economically important insect pests.
Innovation Solution
Modification of Vip3 polypeptides by incorporating heterologous carbohydrate binding modules (CBMs) to enhance their insecticidal activity, including against Vip3-resistant fall armyworms, through the substitution or alteration of specific domains.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If Vip3 proteins are used for insect control, then protection against certain lepidopteran pests is achieved, but effectiveness against Vip3-resistant fall armyworms is lost
Solution Approach 1:
The patent modifies the Vip3 protein structure by substituting Domain III with heterologous carbohydrate binding modules (CBMs) from different sources. This structural parameter change creates new protein variants (Vip3-CBM chimeras) with altered insecticidal properties that overcome resistance in fall armyworm populations while maintaining activity against other lepidopteran pests.
Solution Approach 2:
The invention creates composite protein structures by fusing the Vip3 protein backbone with heterologous CBM domains from diverse organisms including bacteria, fungi, and plants. These chimeric proteins combine the insecticidal domain (I and II) with novel carbohydrate-binding domains to generate enhanced spectral activity and overcome resistance mechanisms.
2Productivity
If Vip3 proteins are expressed in transgenic crops, then pest control is provided, but resistance development in target pests occurs
Solution Approach 1:
The patent employs a dynamic approach by creating multiple Vip3-CBM variant proteins with different CBM domains that can be deployed in rotation or combination. This dynamic protein portfolio strategy prevents resistance fixation in pest populations by continuously presenting novel target structures that pests cannot adapt to simultaneously.
Solution Approach 2:
The invention modifies specific local regions of the Vip3 protein (Domain III) while preserving the essential insecticidal domains (I and II). This localized modification approach maintains core toxicity mechanisms while altering carbohydrate recognition specificity, thereby preserving efficacy against susceptible pests and overcoming resistance in resistant populations.
3Reliability
If Domain III of Vip3 is substituted with heterologous CBMs, then insecticidal activity against resistant strains is enhanced, but protein structure complexity increases
Solution Approach 1:
The Vip3 protein is segmented into functional domains, with Domain III being the substitutable region. This segmentation allows independent modification of the carbohydrate-binding region while preserving the intact toxic core domains (I and II), enabling systematic creation of variants with different CBM domains to target resistant pest populations.
Data Source
AI summary
The present invention is directed to vegetative insecticidal proteins (Vips) modified to comprise heterologous carbohydrate binding modules and methods of use thereof.