ArticleInternational journal of molecular sciences2017
Molecular Basis for the Neutralization of Tumor Necrosis Factor α by Certolizumab Pegol in the Treatment of Inflammatory Autoimmune Diseases.
Article in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 42 citations in OpenAlex.
- Hybrid Supercharged Antibodies: A Rational Approach to Boost Immunoassay Sensitivity via Controlled Nanoparticle Adsorption.Langmuir : the ACS journal of surfaces and colloids · 2026Article
- Biological Treatment of Psoriasis-Data So Far.Pharmaceuticals (Basel, Switzerland) · 2026Review
- The structural basis for the selective antagonism of soluble TNF-alpha by shark variable new antigen receptors.Nature communications · 2025Article
- Rapid, Single-Step Monitoring of Monoclonal Antibody Bioavailability by Using a TNF-α-Based Multiepitope DNA Nanoswitch.Analytical chemistry · 2025Article
- Monoclonal Antibodies for the Treatment of Ocular Diseases.Journal of clinical medicine · 2024Review
- Structure-based development of a canine TNF-α-specific antibody using adalimumab as a template.Protein science : a publication of the Protein Society · 2024Article
- Article
- Crystal structures and molecular dynamics simulations of a humanised antibody fragment at acidic to basic pH.Scientific reports · 2023Article
- Phase I trial of the TNF-α inhibitor certolizumab plus chemotherapy in stage IV lung adenocarcinomas.Nature communications · 2022Article
- Receptor Specificity Engineering of TNF Superfamily Ligands.Pharmaceutics · 2022Review
- Missense variants in the TNFA epitopes and their effects on interaction with therapeutic antibodies-in silico analysis.Journal, genetic engineering & biotechnology · 2022Article
- Higher Affinity Antibodies Bind With Lower Hydration and Flexibility in Large Scale Simulations.Frontiers in immunology · 2022Article
- Hallucinating structure-conditioned antibody libraries for target-specific binders.Frontiers in immunology · 2022Article
- New cembrane-type diterpenoids with anti-inflammatory activity from the South China Sea soft coralBeilstein journal of organic chemistry · 2022Article
- Golimumab (anti-TNF monoclonal antibody): where we stand today.Human vaccines & immunotherapeutics · 2021Review
- Engineering the Fab fragment of the anti-IgE omalizumab to prevent Fab crystallization and permit IgE-Fc complex crystallization.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structural Basis for How Biologic Medicines Bind their Targets in Psoriasis Therapy.The Yale journal of biology and medicine · 2020Article
- An Anti-hTNF-α Variable New Antigen Receptor Format Demonstrates SuperiorFrontiers in immunology · 2019Article
- Structural basis for tumor necrosis factor blockade with the therapeutic antibody golimumab.Protein science : a publication of the Protein Society · 2018Article
- BAFF-neutralizing interaction of belimumab related to its therapeutic efficacy for treating systemic lupus erythematosus.Nature communications · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoclonal antibodies against TNFα, including infliximab, adalimumab, golimumab, and certolizumab pegol, are widely used for the treatment of the inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. Recently, the crystal structures of TNFα, in complex with the Fab fragments of infliximab and adalimumab, have revealed the molecular mechanisms of these antibody drugs. Here, we report the crystal structure of TNFα in complex with the Fab fragment of certolizumab pegol to clarify the precise antigen-antibody interactions and the structural basis for the neutralization of TNFα by this therapeutic antibody. The structural analysis and the mutagenesis study revealed that the epitope is limited to a single protomer of the TNFα trimer. Additionally, the DE loop and the GH loop of TNFα play critical roles in the interaction with certolizumab, suggesting that this drug exerts its effects by partially occupying the receptor binding site of TNFα. In addition, a conformational change of the DE loop was induced by certolizumab binding, thereby interrupting the TNFα-receptor interaction. A comprehensive comparison of the interactions of TNFα blockers with TNFα revealed the epitope diversity on the surface of TNFα, providing a better understanding of the molecular mechanism of TNFα blockers. The accumulation of these structural studies can provide a basis for the improvement of therapeutic antibodies against TNFα.
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