ArticlemAbs2015
Protein design of IgG/TCR chimeras for the co-expression of Fab-like moieties within bispecific antibodies.
Article in mAbs, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Folding-mediated secretion of pure bispecific antibodies.Nature biotechnology · 2026Article
- Generation of mixed-valency, modular multispecific antibodies using disulfide-linked Fc-FcγR complexes.Nature communications · 2026Article
- Rapid affinity-based purification of multi-specific antibodies using Kappa Select and Protein L.mAbs · 2025Article
- Bispecific immunotherapy based on antibodies, T-cell receptors, and aptamers: mechanisms of action, adverse effects, and future perspectives.Frontiers in immunology · 2025Review
- Design and engineering of bispecific antibodies: insights and practical considerations.Frontiers in bioengineering and biotechnology · 2024Review
- Generation of bispecific antibodies by structure-guided redesign of IgG constant regions.Frontiers in immunology · 2022Article
- A new approach to produce IgGScientific reports · 2021Article
- Soluble Expression of Fc-Fused T Cell Receptors Allows Yielding Novel Bispecific T Cell Engagers.Biomedicines · 2021Article
- Recent Advances in the Molecular Design and Applications of Multispecific Biotherapeutics.Antibodies (Basel, Switzerland) · 2021Review
- Computational stabilization of T cell receptors allows pairing with antibodies to form bispecifics.Nature communications · 2020Article
- 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
- Engineering IgG-Like Bispecific Antibodies-An Overview.Antibodies (Basel, Switzerland) · 2018Review
- Article
- Article
- Fab-based bispecific antibody formats with robust biophysical properties and biological activity.mAbs · 2015Article
- Article
- Review
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Immunoglobulins and T cell receptors (TCRs) share common sequences and structures. With the goal of creating novel bispecific antibodies (BsAbs), we generated chimeric molecules, denoted IgG_TCRs, where the Fv regions of several antibodies were fused to the constant domains of the α/β TCR. Replacing CH1 with Cα and CL with Cβ, respectively, was essential for achieving at least partial heavy chain/light chain assembly. Further optimization of the linker regions between the variable and constant domains, as well as replacement of the large FG loop of Cβ with a canonical β-turn, was necessary to consistently obtain full heavy chain/light chain assembly. The optimized IgG_TCR molecules were evaluated biophysically and shown to maintain the binding properties of their parental antibodies. A few BsAbs were generated by co-expressing native Fabs and IgG_TCR Fabs within the same molecular construct. We demonstrate that the IgG_TCR designs steered each of the light chains within the constructs to specifically pair with their cognate heavy chain counterparts. We did find that even with complete constant domain specificity between the CH1/CL and Cα/Cβ domains of the Fabs, strong variable domain interactions can dominate the pairing specificity and induce some mispairing. Overall, the IgG_TCR designs described here are a first step toward the generation of novel BsAbs that may be directed toward the treatment of multi-faceted and complex diseases.
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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.