Fusion Polypeptide Multimerization Domain for Antibody Detection
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Solution Overview
Problem
Current methods for producing multimeric antigens for detecting IgM and IgG antibodies are labor-intensive, time-consuming, and result in inconsistent epitope accessibility due to aggregation issues, affecting the reliability of infection stage differentiation in serological tests.
Innovation Solution
Development of fusion polypeptides with multimerization domains that form stable, soluble multimers through non-covalent interactions, allowing for high-yield, reproducible production and improved epitope accessibility for antibody binding, enabling differential detection of IgM antibodies in infection stages.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If chemical crosslinking is used to produce multimeric antigens, then antigen oligomerization is achieved, but the process becomes labor-intensive and time-consuming with inconsistent results
Solution Approach 1:
The patent introduces a multimerization domain as an intermediary component that mediates the formation of multimeric antigens. This domain acts as a self-organizing element that automatically assembles multiple antigen copies into multimers through non-covalent interactions, eliminating the need for labor-intensive chemical crosslinking procedures while ensuring consistent and reproducible multimer formation across different production batches.
Solution Approach 2:
The multimerization domain enables the antigen system to self-assemble into multimeric structures through intrinsic non-covalent interactions. The system serves itself by automatically organizing into the desired multimeric configuration without requiring external chemical crosslinking agents or complex optimization procedures, thereby reducing both time and labor投入 while improving reproducibility.
2Measurement precision
If high epitope concentration is used in detection antigen, then IgM recognition is improved, but IgG detection becomes unreliable due to epitope accessibility issues
Solution Approach 1:
The patent applies local quality by creating spatially distinct epitope environments within the multimeric antigen structure. Different regions of the multimer present epitopes with varying accessibility characteristics - some epitopes are highly accessible for IgM binding while others maintain appropriate accessibility for IgG recognition. This local differentiation allows simultaneous optimization for both IgM and IgG detection without mutual interference.
3Stability of the object's composition
If higher degree of crosslinking is applied to increase multimerization, then antigen oligomerization improves, but solubility decreases leading to test performance problems
Solution Approach 1:
The patent changes the fundamental parameter of intermolecular interaction from covalent bonding to non-covalent interactions. This parameter change allows the multimeric structure to maintain stability through collective weak interactions while preserving solubility, as non-covalent interactions are reversible and do not create the insolubility issues associated with extensive chemical crosslinking. The multimerization domain is designed to optimize the balance between stability and solubility through controlled non-covalent assembly.
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 fusion polypeptides provide stable and soluble multimers with controlled epitope density, enhancing the specificity and reliability of antibody detection, particularly for early and acute infections, while minimizing interference from other antibody classes.
Implementation Method 1
The fusion polypeptide molecules are capable of forming a multimer. A multimer comprises a plurality of monomeric subunits associated by non-covalent interactions via the multimerization domain.
Data Source
AI summary
The present invention relates to fusion proteins suitable as test antigens in the detection of infections with pathogens, particularly of primary infections with pathogens. Further, the invention relates to methods for detecting and differentially determining antibodies, particularly IgM antibodies resulting from an infection with a pathogenic organism. Furthermore, test reagents for carrying out these methods are provided.