Anti-VSIG4 Antibody Binding Both Protein Isoforms
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Solution Overview
Problem
Current anti-VSIG4 antibodies only bind to one form of the protein, leading to partial inhibition of VSIG4 activity and insufficient activation of immune responses for cancer treatment.
Innovation Solution
Development of a monoclonal antibody that specifically binds to both long and short forms of VSIG4, utilizing specific heavy-chain and light-chain complementarity-determining regions (CDRs) to efficiently suppress VSIG4-mediated anti-inflammatory signals and activate immune responses.
Engineering Contradictions & Design Principles
Engineering Contradiction Analysis
1Reliability
If existing anti-VSIG4 antibodies are used, then some VSIG4 activity is inhibited, but only one form of the protein is bound leading to partial inhibition and insufficient immune activation
Solution Approach 1:
The patent develops a monoclonal antibody (h6F10) that universally binds to both long and short forms of VSIG4 protein, making the antibody versatile across different protein isoforms. This multi-form binding capability resolves the contradiction by enabling the single antibody to inhibit all VSIG4-mediated immune suppression pathways, achieving complete rather than partial inhibition.
2Reliability
If a monoclonal antibody binds to both long and short forms of VSIG4, then complete inhibition of VSIG4 activity is achieved, but antibody design complexity increases
Solution Approach 1:
The patent employs parameter changes in the antibody's complementarity-determining regions (CDRs), specifically optimizing the amino acid sequences in CDR-H3 and CDR-L3 to enable broad recognition of both VSIG4 isoforms. By adjusting these critical binding parameters, the antibody achieves universal binding without requiring complex multi-antibody formulations or engineered chimeric structures.
3Reliability
If VSIG4-mediated anti-inflammatory signals are suppressed, then anti-tumor immunity is enhanced, but non-specific immune inhibition may occur
Solution Approach 1:
The patent achieves selective suppression of VSIG4-mediated immune inhibition through the h6F10 antibody's specific binding to the VSIG4 protein structure. The antibody's CDR regions are precisely configured to recognize epitopes present in both VSIG4 isoforms, enabling localized and specific interference with the VSIG4-T cell receptor interaction pathway without broadly affecting other immune checkpoint pathways or inflammatory processes.
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 novel antibody effectively inhibits VSIG4 activity, promoting anti-tumor immunity by binding to both forms of the protein, inducing internalization and reducing surface expression, thereby enhancing immune activation and cytokine release.
Implementation Method 1
The antibody disclosed herein binds both the long and the short forms of VSIG4
Implementation Method 2
inducing internalization and reducing surface expression
Data Source
AI summary
New anti-VSIG4 (V-set Ig domain-containing 4) antibodies or an antigen-binding fragments are disclosed. Uses of these antibodies, including methods of treatment, are also provided.