Diguetoxin Variant Polypeptides for Resistant Insect Control
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Solution Overview
Problem
Current methods are inadequate in effectively controlling and managing deleterious insects that pose threats to human health and food security, as they are vectors for diseases and pests that cause significant damage to crops and domesticated animals.
Innovation Solution
Development of a diguetoxin variant polypeptide (DVP) with insecticidal activity, comprising specific amino acid sequences and their expression in plants, along with methods for production and application to combat insect pests, including a composition of DVP and excipients, and a yeast strain for expressing the DVP.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If current insect control methods are used, then existing pest management approaches are applied, but they are inadequate in effectively controlling and managing deleterious insects
Solution Approach 1:
The patent applies parameter changes by modifying the amino acid sequence of the diguetoxin polypeptide to create variants with improved insecticidal activity. Specific substitutions at positions 38, 41, 51, and other locations optimize the protein's effectiveness against resistant insect populations while maintaining its core function, thereby resolving the contradiction between reliability and adaptability in pest control.
Solution Approach 2:
The patent creates composite insect control solutions by combining the diguetoxin polypeptide with excipients to form compositions with enhanced stability and efficacy. This composite approach allows the active ingredient to work more effectively against diverse insect pests, addressing both the reliability and adaptability requirements simultaneously.
2Reliability
If diguetoxin variant polypeptide is developed with specific amino acid substitutions, then insecticidal activity is enhanced, but protein expression and stability may be affected
Solution Approach 1:
The patent carefully selects amino acid substitutions that enhance insecticidal activity while preserving protein stability. The modifications at key positions are designed to optimize binding affinity to insect targets without disrupting the overall protein structure, thus resolving the contradiction between enhanced activity and maintained stability.
Solution Approach 2:
The patent incorporates stabilizing amino acid substitutions that preemptively protect the polypeptide from degradation. These protective modifications are built into the protein structure beforehand, cushioning against potential instability issues that might arise from the insecticidal activity-enhancing substitutions, thereby maintaining both activity and stability.
3Stability of the object's composition
If wild-type diguetoxin sequence is used, then natural protein structure is maintained, but insecticidal activity against resistant pests is reduced
Solution Approach 1:
The patent applies local quality changes by introducing specific amino acid substitutions at critical positions within the diguetoxin sequence. These localized modifications enhance insecticidal activity against resistant pests while leaving the overall protein structure intact. The changes are confined to specific regions that interact with insect targets, preserving global structural integrity while achieving enhanced local functionality.
Data Source
AI summary
New insecticidal peptides, polypeptides, proteins, and nucleotides; their expression in culture and plants; methods of producing the peptides, polypeptides, proteins, and nucleotides; new processes; new production techniques; new formulations; and new organisms, are disclosed. The present disclosure is also related to a novel type of peptide named Dc1a-Variant Polypeptides (DVPs) that are a non-naturally occurring, modified-form of the peptide, Mu-diguetoxin-Dc1a, isolated from the American Desert Spider (Diguetia canities). Here we describe: genes encoding DVPs; various formulations and combinations of both genes and peptides; and methods for using the same that are useful for the control of insects. Further, the present invention relates to novel, recombinant cysteine rich proteins (CRPs) with a cystine knot (CK) architecture, created by removing one or more disulfide bonds from a polypeptide having four or more disulfide bonds.