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Updated: Jun 25, 2026

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Generation of Murine Monoclonal Antibodies by Hybridoma Technology
Published on: January 2, 2017
Deimmunization of monoclonal antibodies
Tim D Jones1, Laura J Crompton, Frank J Carr
1Antitope Ltd., Babraham, Cambridge, UK.
Methods in Molecular Biology (Clifton, N.J.)
|March 3, 2009
Summary
Deimmunization removes T-cell epitopes from therapeutic proteins, reducing immune responses. This method creates deimmunized antibodies with retained binding affinity for improved therapies.
Area of Science:
- Immunology
- Biotechnology
- Protein Engineering
Background:
- Immunogenicity, triggered by T-cell epitopes in therapeutic proteins, limits treatment efficacy.
- Helper T-cells recognize these epitopes, leading to antibody production and therapeutic neutralization.
Purpose of the Study:
- To detail a method for creating deimmunized antibodies for mammalian cell production.
- To address the challenge of immunogenicity in protein-based therapeutics.
Main Methods:
- Deimmunization technology combines immunological and molecular biology techniques.
- Identifies and removes T-cell epitopes from protein sequences.
- Introduces mutations to eliminate epitopes while preserving antibody binding affinity.
Main Results:
- Deimmunized antibodies are created using human constant regions.
- Gene expression in mammalian cells facilitates the production of these modified antibodies.
- The described method enables the creation of therapeutic proteins with reduced immunogenicity.
Conclusions:
- Deimmunization is a viable strategy to overcome therapeutic protein immunogenicity.
- This approach allows for the development of safer and more effective antibody therapies.
- The method facilitates the production of deimmunized antibodies in mammalian systems.
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