ArticlemAbs2016
Comparing domain interactions within antibody Fabs with kappa and lambda light chains.
Article in mAbs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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
20 citing papers in PubMed, 35 citations in OpenAlex.
- Article
- Development of a Chicken Immunoglobulin Heavy Chain Variable Region (VH) Single-Domain Antibody (sdAb) Against Calsequestrin (CSQ) and Its Application.Antibodies (Basel, Switzerland) · 2025Article
- New insights into antibody structure with implications for specificity, variable region restriction and isotype choice.Nature reviews. Immunology · 2025Review
- Light Chain Isotype and Antibody-Specificity Impact on Virus Neutralization.Antibodies (Basel, Switzerland) · 2025Article
- The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.Proteins · 2025Article
- Single-residue engineering of lambda (λ) antibody light chains reduces conformational flexibility and enhances thermal stability.Computational and structural biotechnology journal · 2025Article
- Thermostability and binding properties of single-chained Fv fragments derived from therapeutic antibodies.Protein science : a publication of the Protein Society · 2024Article
- Design of an alternate antibody fragment format that can be produced in the cytoplasm of Escherichia coli.Scientific reports · 2023Article
- Structural mechanism of Fab domain dissociation as a measure of interface stability.Journal of computer-aided molecular design · 2023Article
- One-Step Homogeneous Immunoassay for the Detection of Influenza Virus Using Switching Peptide and Graphene Quencher.Biochip journal · 2022Article
- Computational stabilization of T cell receptors allows pairing with antibodies to form bispecifics.Nature communications · 2020Article
- Specific Targeting of Lymphoma Cells Using Semisynthetic Anti-Idiotype Shark Antibodies.Frontiers in immunology · 2020Article
- Article
- Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains.Scientific reports · 2019Article
- Native Human Monoclonal Antibodies with Potent Cross-Lineage Neutralization of Influenza B Viruses.Antimicrobial agents and chemotherapy · 2018Article
- The effects of Antibody Engineering CH and CL in Trastuzumab and Pertuzumab recombinant models: Impact on antibody production and antigen-binding.Scientific reports · 2018Article
- Computational design of a specific heavy chain/κ light chain interface for expressing fully IgG bispecific antibodies.Protein science : a publication of the Protein Society · 2017Article
- EFab domain substitution as a solution to the light-chain pairing problem of bispecific antibodies.mAbsArticle
- Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
IgG antibodies are multi-domain proteins with complex inter-domain interactions. Human IgG heavy chains (HCs) associate with light chains (LCs) of the κ or λ isotype to form mature antibodies capable of binding antigen. The HC/LC interaction involves 4 domains: VH and CH1 from the HC and VL and CL from the LC. Human Fabs with κ LCs have been well characterized for their unfolding behaviors and demonstrate a significant level of cooperativity and stabilization when all 4 domains are intact. Very little is known regarding the thermodynamic properties of human Fabs with λ LCs. Here, we dissect the domain contributions to Fab stability for both κ and λ LC-containing Fabs. We find the cooperativity of unfolding between the constant domains, CH1/Cλ, and variable domains, VH/Vλ, within λ LC-containing Fabs is significantly weaker than that of κ LC-containing Fabs. The data suggests there may not be an evolutionary necessity for strong variable/constant domain cooperativity within λ LC-containing Fabs. After investigating the biophysical properties of Fabs with mismatched variable and constant domain subunits (e.g., VH/Vκ paired with CH1/Cλ or T cell receptor Cα/Cβ), the major role of the constant domains for both κ- and λ-containing Fabs may be to reduce the hydrophobic exposure at the VH/VL interface. Even though Fabs with these non-native pairings were thermodynamically less stable, they secreted well from mammalian cells as well behaved monodisperse proteins, which was in contrast to what was observed with the VH/Vκ and VH/Vλ scFvs that secreted as a mixture of monomer and aggregates.
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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.