Anti-VSIG4 Monoclonal Antibody Binding Both Protein Forms

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Solution Overview

Problem

Current anti-VSIG4 antibodies only bind one form of the protein, leading to partial inhibition of VSIG4 activity and lack application in cancer treatment, as they do not effectively suppress VSIG4-mediated anti-inflammatory signals or revert inhibition of T-cell activation.

Innovation Solution

Development of a monoclonal antibody specifically binding to both long and short forms of VSIG4, with specific heavy-chain and light-chain complementarity-determining regions (CDRs) sequences, to efficiently suppress VSIG4-mediated anti-inflammatory signals and repolarize tumor-associated macrophages to a tumour suppressive M1 phenotype, thereby activating an immune response and conferring protective anti-tumor immunity.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If current anti-VSIG4 antibodies are used, then they can bind to VSIG4 protein, but they only bind one form of the protein (long or short form) leading to partial inhibition of VSIG4 activity

Engineering Contradiction:
Improveinhibition efficacy of VSIG4 activityVSAvoidbinding capability to different VSIG4 forms
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The patent develops a monoclonal antibody (designated as antibody or antigen-binding fragment thereof) that universally binds to both the long form and short form of VSIG4 protein. This universal binding capability allows the antibody to effectively inhibit VSIG4-mediated anti-inflammatory signals regardless of which form is present, thereby achieving complete functional inhibition rather than partial inhibition.

Inventive Principle:
Principle #6Universality (Multi-functionality)

Solution Approach 2:

The patent identifies and utilizes specific complementarity-determining region (CDR) sequences in the antibody variable regions that enable recognition and binding to both VSIG4 forms. By optimizing the CDR sequences (particularly CDR-H3 and CDR-L3), the antibody achieves enhanced affinity and specificity for both protein forms, transforming the binding parameter to accommodate multiple targets.

Inventive Principle:
Principle #35Parameter changes

2Ease of manufacture

If current anti-VSIG4 antibodies are used, then they can be produced as immunotherapeutic agents, but they lack application in cancer treatment due to insufficient suppression of anti-inflammatory signals and T-cell activation inhibition

Engineering Contradiction:
Improveproducibility as immunotherapeutic agentVSAvoidtherapeutic effectiveness in cancer treatment
Core Design Contradiction:
Ease of manufactureVSReliability

Solution Approach 1:

The patent optimizes the antibody's biological function by selecting specific CDR sequences that enhance its ability to block VSIG4-mediated immune suppression. This parameter optimization ensures the antibody can effectively suppress anti-inflammatory signals and reverse T-cell activation inhibition, meeting the therapeutic requirements for cancer treatment while maintaining manufacturability.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent provides a complete antibody sequence specification including variable and constant regions, enabling straightforward recombinant production. This detailed sequence information allows for efficient manufacturing of the therapeutic antibody without requiring complex production processes, making the drug development economically viable.

Inventive Principle:
Principle #27Cheap short-living objects (Disposable)

Data Source

PatentUS20240158503A1Anti-VSIG4 antibody or antigen binding fragment and uses thereof
Publication Date: 2024.05.16 PIERRE FABRE MEDICAMENT SAS
  • US20240158503A1 patent drawing
  • US20240158503A1 patent drawing
  • US20240158503A1 patent drawing

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.