ArticlemAbs
EFab domain substitution as a solution to the light-chain pairing problem of bispecific antibodies.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Folding-mediated secretion of pure bispecific antibodies.Nature biotechnology · 2026Article
- Bispecific Antibodies in Breast Cancer Immunotherapy: Mechanisms, Advances, and Translational Challenges.Targeted oncology · 2026Review
- Article
- IgE based therapeutics are an emerging modality in cancer treatment.Discover oncology · 2025Review
- Mechanism of Action and Pharmacokinetics of Approved Bispecific Antibodies.Biomolecules & therapeutics · 2024Review
- Serum immunoglobulin or albumin binding single-domain antibodies that enable tailored half-life extension of biologics in multiple animal species.Frontiers in immunology · 2024Article
- Dual reactivity disulfide bridging reagents; enabling new approaches to antibody fragment bioconjugation.Chemical science · 2022Article
- A human IgE bispecific antibody shows potent cytotoxic capacity mediated by monocytes.The Journal of biological chemistry · 2022Article
- Article
- Bispecific antibodies: a mechanistic review of the pipeline.Nature reviews. Drug discovery · 2019Review
- Diabody-Ig: a novel platform for the generation of multivalent and multispecific antibody molecules.mAbs · 2019Article
- Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bispecific antibody therapeutics can expand the functionality of a conventional monoclonal antibody drug because they can bind multiple antigens. However, their great potential is counterbalanced by the challenges faced in their production. The classic asymmetric bispecific containing an Fc requires the expression of four unique chains - two light chains and two heavy chains; each light chain must pair with its correct heavy chain, which then must heterodimerize to form the full bispecific. The light-chain pairing problem has several solutions, some of which require engineering and optimization for each bispecific pair. Here, we introduce a technology called EFab Domain Substitution, which replaces the Cε2 of IgE for one of the CL/CH1 domains into one arm of an asymmetric bispecific to encourage the correct pairing of the light chains. EFab Domain Substitution provides very robust correct pairing while maintaining antibody function and is effective for many variable domains. We report its effect on the biophysical properties of an antibody and the crystal structure of the EFab domain substituted into the adalimumab Fab (PDB ID 6CR1).
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.