Chimeric Cry1 Proteins for Lepidopteran Pest Control
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Solution Overview
Problem
Current pest control methods, including chemical and biological agents, face challenges in effectively targeting a wide spectrum of economically important insect pests and managing resistance in pest populations.
Innovation Solution
Development of novel chimeric pesticidal proteins, specifically designed to target lepidopteran insect pests, including those resistant to existing Vip3A and Cry1F proteins, by fusing N-terminal and C-terminal regions of different Cry1 proteins at a crossover position within conserved block 3.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing Cry1 proteins are used to control lepidopteran pests, then insecticidal activity is achieved, but resistance development in pest populations occurs
Solution Approach 1:
The patent combines N-terminal and C-terminal regions of different Cry1 proteins (Cry1A, Cry1C, Cry1E, Cry1F) to create chimeric proteins that exhibit enhanced insecticidal activity against lepidopteran pests while managing resistance. The chimeric structure merges functional domains from multiple parent proteins to achieve both potency and resistance management.
Solution Approach 2:
The invention modifies specific regions of the Cry1 protein structure by replacing certain domains with homologous regions from other Cry1 variants. This local substitution approach allows optimization of insecticidal activity in specific domains while maintaining overall protein function and addressing resistance issues through localized structural changes.
2Adaptability or versatility
If a broad spectrum of insect pests is targeted, then pest control effectiveness is improved, but specificity to non-target organisms may be compromised
Solution Approach 1:
The patent creates chimeric Cry1 proteins with modified amino acid sequences that alter the protein's structural parameters and binding characteristics. These parameter changes enable the chimeric proteins to recognize and bind to a broader range of insect receptors while maintaining selectivity through preserved critical binding domains, thus expanding spectrum without compromising safety.
3Reliability
If Cry proteins are engineered to enhance activity, then insecticidal potency is improved, but protein complexity increases
Solution Approach 1:
The chimeric Cry1 proteins are constructed by segmenting the protein into distinct functional domains (N-terminal region, core domain, C-terminal region) and recombining these segments from different parent proteins. This modular segmentation allows systematic optimization of insecticidal activity while maintaining structural organization and facilitating rational design of enhanced variants.
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 chimeric insecticidal proteins demonstrate enhanced activity against target insect pests, including resistant strains, offering a broader spectrum of control and reducing the development of resistance.
Implementation Method 1
The protoxins are processed by proteases in the insect gut, for example trypsin and chymotrypsin, to produce a protease-resistant core Cry protein toxin.
Implementation Method 2
Domain I, typically consists of seven alpha helices and is involved in membrane insertion and pore formation.
Data Source
AI summary
The invention provides nucleic acids, polypeptides, transgenic plants, compositions and methods for conferring pesticidal activity (e.g., insecticidal activity) to bacteria, plants, plant cells, tissues and seeds. Nucleic acids encoding the insecticidal proteins can be used to transform prokaryotic and eukaryotic organisms to express the insecticidal proteins. The recombinant organisms or compositions containing the recombinant organisms or insecticidal proteins or in combination with an appropriate agricultural carrier can be used to control an insect pest in various environments.