ArticleJournal of molecular biology2015
An improved single-chain Fab platform for efficient display and recombinant expression.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
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- Intravaginal delivery of mRNA-encoded antibodies with enhanced breadth and potency for SHIV/HIV protection.Nature communications · 2025Article
- MicroRNA-142 improves IL1RAP CAR-T cell activity in acute myeloid leukemia.Journal of hematology & oncology · 2025Article
- Single-chain Fab chain-exchange (scFab-PACE) converts targeted prodrugs into functional T cell engagers on tumor cells.The Journal of biological chemistry · 2025Article
- Multilayered HIV-1 resistance in HSPCs through CCR5 Knockout and B cell secretion of HIV-inhibiting antibodies.Nature communications · 2025Article
- Fluorescein-based SynNotch adaptors for regulating gene expression responses to diverse extracellular and matrix-based cues.Nature communications · 2025Article
- Mutability and hypermutation antagonize immunoglobulin codon optimality.Molecular cell · 2025Article
- Mechanistic computational modeling of monospecific and bispecific antibodies targeting interleukin-6/8 receptors.PLoS computational biology · 2024Article
- Multiparatopic antibodies induce targeted downregulation of programmed death-ligand 1.Cell chemical biology · 2024Article
- A mammalian cell display platform based on scFab transposition.Antibody therapeutics · 2023Article
- Engineered bispecific antibodies targeting the interleukin-6 and -8 receptors potently inhibit cancer cell migration and tumor metastasis.Molecular therapy : the journal of the American Society of Gene Therapy · 2022Article
- SARS-CoV-2 reactive and neutralizing antibodies discovered by single-cell sequencing of plasma cells and mammalian display.Cell reports · 2022Article
- The mosaic puzzle of the therapeutic monoclonal antibodies and antibody fragments - A modular transition from full-length immunoglobulins to antibody mimetics.Leukemia research reports · 2022Article
- Development of Antibody-Based PROTACs for the Degradation of the Cell-Surface Immune Checkpoint Protein PD-L1.Journal of the American Chemical Society · 2021Article
- A phage-displayed single-chain Fab library optimized for rapid production of single-chain IgGs.Protein science : a publication of the Protein Society · 2020Article
- Molecular Engineering Strategies Tailoring the Apoptotic Response to a MET Therapeutic Antibody.Cancers · 2020Article
- Advances in the Production and Batch Reformatting of Phage Antibody Libraries.Molecular biotechnology · 2019Review
- A Human IgE Antibody Binding Site on Der p 2 for the Design of a Recombinant Allergen for Immunotherapy.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- On a Robust, Sensitive Cell-Free Method forMicromachines · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Antibody phage display libraries combined with high-throughput selections have recently demonstrated tremendous promise to create the next generation of renewable, recombinant antibodies to study proteins and their many post-translational modification states; however, many challenges still remain, such as optimized antibody scaffolds. Recently, a single-chain fragment antigen binding (Fab) (scFab) format, in which the carboxy-terminus of the light chain is linked to the amino-terminus of the heavy chain, was described to potentially combine the high display levels of a single-chain fragment variable with the high stability of purified Fabs. However, this format required removal of the interchain disulfide bond to achieve modest display levels and subsequent bacterial expression resulted in high levels of aggregated scFab, hindering further use of scFabs. Here, we developed an improved scFab format that retains the interchain disulfide bond by increasing the linker length between the light and heavy chains to improve display and bacterial expression levels to 1-3 mg/L. Furthermore, rerouting of the scFab to the co-translational signal recognition particle pathway combined with reengineering of the signal peptide sequence results in display levels 24-fold above the original scFab format and 3-fold above parent Fab levels. This optimized scFab scaffold can be easily reformatted in a single step for expression in a bacterial or mammalian host to produce stable (Tm of 81 °C), predominantly monomeric (>90%) antibodies at a high yield. Ultimately, this new scFab format will advance high-throughput antibody generation platforms to discover the next generation of research and therapeutic antibodies.
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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.