Fully Humanized Anti-TLR2 Antibodies

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Solution Overview

Problem

Current monoclonal antibodies targeting Toll-like Receptor 2 (TLR2) often induce human anti-mouse antibody (HAMA) responses, leading to reduced therapeutic efficacy due to their rodent origin, and existing humanization techniques like chimerism and CDR grafting may impair binding affinity and immunogenicity.

Innovation Solution

Development of fully humanized monoclonal antibodies with specific amino acid sequences for the light and heavy chains that are entirely of human origin, devoid of murine residues, capable of binding to human TLR2 and neutralizing its activity without requiring CD32 binding, thus minimizing immunogenicity and maintaining high affinity.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If rodent monoclonal antibodies are used to target TLR2, then binding specificity and therapeutic effect are achieved, but human anti-mouse antibody (HAMA) responses are induced leading to reduced therapeutic efficacy

Engineering Contradiction:
Improvetherapeutic efficacyVSAvoidHAMA immune responses
Core Design Contradiction:
ReliabilityVSObject-affected harmful factors

Solution Approach 1:

The patent applies parameter changes by modifying the amino acid sequence composition of the antibody to transition from rodent origin to fully human origin. This involves changing the fundamental parameter of species origin while maintaining the functional parameter of TLR2 binding capability, thereby eliminating HAMA responses while preserving therapeutic efficacy.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

The patent creates a humanized version of the rodent antibody by copying the essential binding characteristics and structural features of the original rodent antibody while replacing the amino acid sequences with human-derived sequences. This allows the antibody to maintain its therapeutic function while being immunologically compatible with humans.

Inventive Principle:
Principle #26Copying

2Object-affected harmful factors

If chimerism or CDR grafting techniques are used to humanize antibodies, then immunogenicity is reduced, but binding affinity and therapeutic effectiveness are impaired

Engineering Contradiction:
ImproveimmunogenicityVSAvoidbinding affinity
Core Design Contradiction:
Object-affected harmful factorsVSReliability

Solution Approach 1:

The patent achieves a superior balance by changing the parameter of amino acid sequence composition to use fully human sequences rather than partial humanization. This complete transformation maintains high binding affinity while maximizing reduction of immunogenicity, overcoming the limitations of incremental humanization approaches.

Inventive Principle:
Principle #35Parameter changes

Solution Approach 2:

Instead of starting with a rodent antibody and partially humanizing it (the conventional approach), the patent inverts the approach by developing de novo fully human antibodies that naturally possess both high human compatibility and high binding affinity, avoiding the inherent trade-offs of partial humanization techniques.

Inventive Principle:
Principle #13The other way round (Inversion)

Data Source

PatentEP2805973B1Humanised antibodies to Toll-like receptor 2 and uses thereof
Publication Date: 2017.11.08 OPSONA THERAPEUTICS
  • EP2805973B1 patent drawingFigure 1A
  • EP2805973B1 patent drawingFigure 1B
  • EP2805973B1 patent drawingFigure 2A

AI summary

A fully humanised antibody having binding specificity to Toll-like Receptor 2 comprising a light chain and a heavy chain entirely comprised of amino acid sequence of human origin. The variable region of the light chain comprises an amino acid sequence which is substantially homologous with the sequence of 5 SEQ ID NO:1, while the variable region of the heavy domain comprises an amino acid sequence which is substantially homologous with the sequence of SEQ ID NO:4. Also provided are nucleic acids encoding such antibodies, as well as the use of the antibodies in medicine, in particular for the treatment of inflammatory and autoimmune diseases which are mediated by Toll-like Receptor 2 activation 10 and signalling.