Multimeric Fusion Protein Glycoengineering for IgG Disorders

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Solution Overview

Problem

Current treatments for IgG-mediated disorders and antibody-mediated injury during organ transplantation are limited in efficacy and specificity, and there is a need for innovative approaches to modulate IgG effector functions.

Innovation Solution

The development of a multimeric fusion protein comprising an antibody heavy chain CH2 and CH3 regions fused with catalytic domains of sialyltransferase and galactosyltransferase, which can be administered to treat IgG-mediated disorders and antibody-mediated injury.

Engineering Contradictions & Design Principles

VSEngineering Contradiction Analysis

1Reliability

If conventional treatments are used for IgG-mediated disorders, then treatment can be provided, but efficacy and specificity are limited

Engineering Contradiction:
Improvetreatment efficacyVSAvoidtreatment specificity
Core Design Contradiction:
ReliabilityVSAdaptability or versatility

Solution Approach 1:

The invention changes the chemical parameters of IgG by enzymatically modifying its glycosylation pattern. Specifically, sialyltransferase and galactosyltransferase enzymes are used to add sialic acid and galactose residues to the IgG glycans, respectively. This parameter change in glycosylation structure transforms the biological activity of IgG, enabling it to modulate effector functions with enhanced efficacy and specificity for treating IgG-mediated disorders

Inventive Principle:
Principle #35Parameter changes

2Reliability

If IgG effector functions are modulated through glycosylation engineering, then treatment efficacy improves, but treatment complexity increases

Engineering Contradiction:
Improvetreatment efficacyVSAvoidtreatment complexity
Core Design Contradiction:
ReliabilityVSDevice complexity

Solution Approach 1:

The invention employs a self-service approach where the therapeutic IgG molecules themselves carry the enzymatic machinery (sialyltransferase and galactosyltransferase domains) required for their own glycosylation modification. This allows the IgG to autonomously modify its own glycan structures in vivo, eliminating the need for complex external enzymatic treatment protocols and reducing overall treatment complexity while maintaining high efficacy

Inventive Principle:
Principle #25Self-service

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 multimeric fusion protein effectively modulates IgG effector functions by sialylating and galactosylating glycoproteins, thereby attenuating autoantibody-mediated inflammation and improving treatment outcomes for IgG-mediated disorders and antibody-mediated injury.

Implementation Method 1

the catalytic domain of sialyltransferase catalyzes sialylation of a glycoprotein

Methodology Applied
Scientific EffectSialylation: Chemical Bonding

Implementation Method 2

the catalytic domain of galactosyltransferase catalyzes galactosylation of a glycoprotein

Methodology Applied
Scientific EffectGalactosylation: Chemical Bonding

Data Source

PatentEP3728570B1glycoengineering
Publication Date: 2025.02.12 THE GENERAL HOSPITAL CORP
  • EP3728570B1 patent drawingFigure 1A~1C
  • EP3728570B1 patent drawingFigure 1D~1E
  • EP3728570B1 patent drawingFigure 2A~2B

AI summary

This disclosure relates to glycoengineering, and methods of utilizing glycoengineering for various therapeutic purposes.