ArticleProtein engineering, design & selection : PEDS2018
Variable heavy-variable light domain and Fab-arm CrossMabs with charged residue exchanges to enforce correct light chain assembly.
Article in Protein engineering, design & selection : PEDS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 23 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Bispecific Antibodies: From Research to Clinical Application.Frontiers in immunology · 2021Pooled it
- IMGT-NC Engineered Variants of INN Therapeutic IG or Antibodies and Related IgSF Proteins (TR, FPIA and CPCA): Bridging Sequences, Structures and Functions for AI.Biomolecules · 2026Review
- Tobemstomig, a Novel Bispecific Antibody, Preferentially Blocks PD-1 and LAG-3 on CD8 TILs to Expand Stem-like T Cells for Sustained Tumor Control.Cancer research communications · 2026Article
- First-in-human study of lomvastomig, a PD-1-TIM-3 bispecific antibody, in patients with advanced and/or metastatic solid tumors.Journal for immunotherapy of cancer · 2026Article
- Optimizing asymmetric antibody purification: a semi-automated process and its digital integration.mAbs · 2025Article
- BAFF-based trifunctional T-cell engagers trigger robust tumor immunity against B-cell malignancies.Protein & cell · 2025Article
- CEA-4-1BBL: CEACAM5-Targeted 4-1BB Ligand Fusion Proteins for Cis Co-Stimulation with CEA-TCB.Antibodies (Basel, Switzerland) · 2025Article
- T-Cell Engagers-The Structure and Functional Principle and Application in Hematological Malignancies.Cancers · 2024Review
- Episomal Vectors for Stable Production of Recombinant Proteins and Engineered Antibodies.Antibodies (Basel, Switzerland) · 2024Article
- End-to-end approach for the characterization and control of product-related impurities in T cell bispecific antibody preparations.International journal of pharmaceutics: X · 2023Article
- Structural mechanism of Fab domain dissociation as a measure of interface stability.Journal of computer-aided molecular design · 2023Article
- Designing of a bispecific antibody against SARS-CoV-2 spike glycoprotein targeting human entry receptors DPP4 and ACE2.Human immunology · 2022Article
- Comparing Antibody Interfaces to Inform Rational Design of New Antibody Formats.Frontiers in molecular biosciences · 2022Article
- Protocols for Rational Design of Protein Solubility and Aggregation Properties Using Aggrescan3D Standalone.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Targeting intracellular WT1 in AML with a novel RMF-peptide-MHC-specific T-cell bispecific antibody.Blood · 2021Article
- Article
- Design and Production of Bispecific Antibodies.Antibodies (Basel, Switzerland) · 2019Review
- Tumor-targeted 4-1BB agonists for combination with T cell bispecific antibodies as off-the-shelf therapy.Science translational medicine · 2019Article
- Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Technologies for the production of bispecific antibodies need to overcome two major challenges. The first one is correct heavy chain assembly, which was solved by knobs-into-holes technology or charge interactions in the CH3 domains. The second challenge is correct light chain assembly. This can be solved by engineering the Fab-arm interfaces or applying the immunoglobulin domain crossover approach. There are three different crossovers possible, namely Fab-arm, constant domain and variable domain crossovers. The CrossMabCH1-CL exchange does not lead to the formation of unexpected side products, whereas the CrossMabFab and the CrossMabVH-VL formats result in the formation of typical side products. Thus, CrossMabCH1-CL was initially favored for therapeutic antibody development. Here, we report a novel improved CrossMab design principle making use of site-specific positional exchanges of charged amino acid pairs in the constant domain of these CrossMabs to enable the correct light chain assembly in the CrossMabVH-VL and improvements for the CrossMabFab design.
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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.