ArticlemAbs
Comprehensive study of domain rearrangements of single-chain bispecific antibodies to determine the best combination of configurations and microbial host cells.
Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Design and Evaluation of Domain-Rearranged Bispecific Antibody Fragments for Functional Optimization.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Cancer therapeutic trispecific antibodies recruiting both T and natural killer cells to cancer cells.Oncology reports · 2023Article
- Functional integration of protein A binding ability to antibody fragments for convenient and tag-free purification.Bioengineered · 2023Article
- Addition of arginine hydrochloride and proline to the culture medium enhances recombinant protein expression in Brevibacillus choshinensis: The case of RBD of SARS-CoV-2 spike protein and its antibody.Protein expression and purification · 2022Article
- T Cell Bispecific Antibodies: An Antibody-Based Delivery System for Inducing Antitumor Immunity.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Anti-EGFR antibody 528 binds to domain III of EGFR at a site shifted from the cetuximab epitope.Scientific reports · 2021Article
- Functional Domain Order of an Anti-EGFR × Anti-CD16 Bispecific Diabody Involving NK Cell Activation.International journal of molecular sciences · 2020Article
- Build-up functionalization of anti-EGFR × anti-CD3 bispecific diabodies by integrating high-affinity mutants and functional molecular formats.Scientific reports · 2020Article
- Bispecific Antibodies and Antibody-Drug Conjugates for Cancer Therapy: Technological Considerations.Biomolecules · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Small bispecific antibodies (bsAbs) are important therapeutic molecules and represent the first bsAb format approved by the United States Food and Drug Administration. Diabody (Db), a small bsAb format, has four possible domain orders; we previously reported the differences in the expression levels and cancer growth inhibition effects upon rearranging the domain order of this format. However, there have been no comprehensive reports on domain rearrangements of bispecific single-chain Db (scDb) and tandem single-chain Fv (taFv), which are widely used bsAb formats. In this study, we designed all possible domain orders for scDb and taFv (each with eight variants) with identical Fv pairs and individually expressed all 16 variants using Escherichia coli, Pichia pastoris, and Brevibacillus choshinensis. Comprehensive investigations showed that the intrinsic functions of the variants were similar to each other, regardless of the expression host system, but expression levels varied depending on the format as well as on the host cell. Among the 16 variants, we found a promising candidate that exhibited high activity and productivity. Furthermore, we determined that B. choshinensis is an attractive expression host because of its secretory production of recombinant proteins.
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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.