ArticleJournal of molecular biology2009
Efficient recovery of high-affinity antibodies from a single-chain Fab yeast display library.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The trial behind it
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
27 citing papers in PubMed.
- Development of ACE2-tropic-betacoronavirus therapeutics for future pandemic preparedness.Nature communications · 2025Article
- Microfluidics combined with electron microscopy for rapid and high-throughput mapping of antibody-viral glycoprotein complexes.Nature biomedical engineering · 2025Article
- High-throughput strategies for monoclonal antibody screening: advances and challenges.Journal of biological engineering · 2025Review
- A mammalian cell display platform based on scFab transposition.Antibody therapeutics · 2023Article
- Increasing sensitivity of antibody-antigen interactions using photo-cross-linking.Cell reports methods · 2023Article
- Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms.Methods in molecular biology (Clifton, N.J.) · 2022Review
- A phage-displayed single-chain Fab library optimized for rapid production of single-chain IgGs.Protein science : a publication of the Protein Society · 2020Article
- Review
- Conjugation of an scFab domain to the oligomeric HIV envelope protein for use in immune targeting.PloS one · 2019Article
- Surface plasmon resonance (SPR) based binding studies of refolded single chain antibody fragments.Biochemistry and biophysics reports · 2018Article
- Fab is the most efficient format to express functional antibodies by yeast surface display.mAbs · 2018Article
- N-terminal residues of an HIV-1 gp41 membrane-proximal external region antigen influence broadly neutralizing 2F5-like antibodies.Virologica Sinica · 2015Article
- CD4 binding site broadly neutralizing antibody selection of HIV-1 escape mutants.The Journal of general virology · 2015Article
- An improved single-chain Fab platform for efficient display and recombinant expression.Journal of molecular biology · 2015Article
- Applications of Yeast Surface Display for Protein Engineering.Methods in molecular biology (Clifton, N.J.) · 2015Review
- Design of an Escherichia coli expressed HIV-1 gp120 fragment immunogen that binds to b12 and induces broad and potent neutralizing antibodies.The Journal of biological chemistry · 2013Article
- Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.Immunological reviews · 2012Review
- Yeast display of engineered antibody domains.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Characteristics of the earliest cross-neutralizing antibody response to HIV-1.PLoS pathogens · 2011Article
- Identification and characterization of Ixodes scapularis antigens that elicit tick immunity using yeast surface display.PloS one · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Yeast display is a powerful technology for the isolation of monoclonal antibodies (mAbs) against a target antigen. Antibody libraries have been displayed on the surface of yeast as both single-chain variable fragment (scFv) and antigen binding fragment (Fab). Here, we combine these two formats to display well-characterized mAbs as single-chain Fabs (scFabs) on the surface of yeast and construct the first scFab yeast display antibody library. When expressed on the surface of yeast, two out of three anti-human immunodeficiency virus (HIV)-1 mAbs bound with higher affinity as scFabs than scFvs. Also, the soluble scFab preparations exhibited binding and neutralization profiles comparable to that of the corresponding Fab fragments. Display of an immune HIV-1 scFab library on the surface of yeast, followed by rounds of sorting against HIV-1 gp120, allowed for the selection of 13 antigen-specific clones. When the same cDNA was used to construct the library in an scFv format, a similar number but a lower affinity set of clones were selected. Based on these results, yeast-displayed scFab libraries can be constructed and selected with high efficiency, characterized without the need for a reformatting step, and used to isolate higher-affinity antibodies than scFv libraries.
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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.