IgG-Specific Enzymes with Reduced Residual Glycan Hydrolysis
Application
Novel enzymes for IgG-specific glycosynthesis.
Key Benefits
- Nearly full glycosylation of IgG antibodies.
- Improved antibody-mediated effector function properties.
- No measurable residual hydrolysis activity.
Market Summary
The global monoclonal antibodies market is experiencing significant growth due to the rising prevalence of chronic diseases such as cancer and cardiovascular conditions. However, existing technologies for modifying IgG antibodies, such as glycosynthases, often suffer from unwanted hydrolytic activity, leading to inefficiencies. A key unmet need remains the development of technologies to optimize monoclonal antibody glycosylation, ensuring better clinical outcomes.
Technical Summary
Emory researchers have developed enzymes that enhance the regulation of antibody-mediated immune responses. These enzymes, known as glycosynthases, exhibit improved transglycosylation functions and reduced residual hydrolytic activity. This advancement was achieved through a novel residue mutation, resulting in IgG-specific glycosynthases with reduced residual glycan hydrolysis. This invention addresses the need for more precise and efficient glycosylation of IgG antibodies, which is essential for improving therapeutic effectiveness and reducing inflammation in autoimmune diseases. By enhancing the glycosynthase function of EndoS2D184M, this technology offers a more effective approach to antibody-based treatments.
Patent Information
| App Type |
Country |
Serial No. |
Patent No. |
File Date |
Issued Date |
Patent Status |
| PCT |
PCT |
PCT/US2024/025296 |
|
4/18/2024 |
|
Pending |
|
|
