ArticleActa pharmaceutica Sinica. B2019
Improvement in affinity and thermostability of a fully human antibody against interleukin-17A by yeast-display technology and CDR grafting.
Article in Acta pharmaceutica Sinica. B, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- EngineeringMicroorganisms · 2026Article
- Cell surface display of VP1 of foot-and-mouth disease virus on Saccharomyces cerevisiae.Microbial cell factories · 2025Article
- Computational refinement and multivalent engineering of complementarity-determining region-grafted nanobodies on a humanized scaffold for retaining antiviral efficacy.Briefings in bioinformatics · 2025Article
- Spinal astrocyte-derived interleukin-17A promotes pain hypersensitivity in bone cancer mice.Acta pharmaceutica Sinica. B · 2024Article
- Quantitative measurement of cell-surface displayed proteins based on split-GFP assembly.Microbial cell factories · 2024Article
- Engineering Strategies to Overcome the Stability-Function Trade-Off in Proteins.ACS synthetic biology · 2022Review
- Yeast Surface Display System: Strategies for Improvement and Biotechnological Applications.Frontiers in bioengineering and biotechnology · 2021Review
- Design of a Trispecific Checkpoint Inhibitor and Natural Killer Cell Engager Based on a 2 + 1 Common Light Chain Antibody Architecture.Frontiers in immunology · 2021Article
- Evaluation ofActa pharmaceutica Sinica. B · 2020Article
- Exploration and Modulation of Antibody Fragment Biophysical Properties by Replacing the Framework Region Sequences.Antibodies (Basel, Switzerland) · 2020Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies (mAbs) are widely used in many fields due to their high specificity and ability to recognize a broad range of antigens. IL-17A can induce a rapid inflammatory response both alone and synergistically with other proinflammatory cytokines. Accumulating evidence suggests that therapeutic intervention of IL-17A signaling offers an attractive treatment option for autoimmune diseases and cancer. Here, we present a combinatorial approach for optimizing the affinity and thermostability of a novel anti-hIL-17A antibody. From a large naïve phage-displayed library, we isolated the anti-IL-17A mAb 7H9 that can neutralize the effects of recombinant human IL-17A. However, the modest neutralization potency and poor thermostability limit its therapeutic applications.
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