ArticleThe Journal of biological chemistry2013
Structural basis for treating tumor necrosis factor α (TNFα)-associated diseases with the therapeutic antibody infliximab.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers, 1 of them a synthesis that pooled it.
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Who cites it
56 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.
- Fourteen small molecule and biological agents for psoriatic arthritis: A network meta-analysis of randomized controlled trials.Medicine · 2020Pooled it
- HDX-MS Detects Steric Protection and Trimeric Compaction of TNFα after It Binds Receptors or Antibodies.ACS omega · 2026Article
- Effect of acetylsalicylic acid (ASA) pretreatment on white noise-induced stress model in rats.BMC veterinary research · 2026Article
- Integrative Computational Prediction Strategy for Antibody-Antigen Binding: A Case Study on Interleukin-1 Beta.Journal of chemical information and modeling · 2026Article
- Molecular determinants of TNFR1:TNFα binding and dynamics in a physiological membrane environment.Current research in structural biology · 2026Article
- The structural basis for the selective antagonism of soluble TNF-alpha by shark variable new antigen receptors.Nature communications · 2025Article
- Design of minibinder proteins as universal antagonists against canine and human TNFα.Communications biology · 2025Article
- Differential Binding of ΔFN3 Proteins ofInternational journal of molecular sciences · 2025Article
- Rapid, Single-Step Monitoring of Monoclonal Antibody Bioavailability by Using a TNF-α-Based Multiepitope DNA Nanoswitch.Analytical chemistry · 2025Article
- Physiologically Based Pharmacokinetic Models for Infliximab, Ipilimumab, and Nivolumab Developed with GastroPlus to Predict Hepatic Concentrations.Pharmaceutics · 2025Article
- The Impact of Infliximab on Hyperinflammation State in Hospitalized COVID-19 Patients: A Retrospective Study.Medicina (Kaunas, Lithuania) · 2024Article
- Thermostability and binding properties of single-chained Fv fragments derived from therapeutic antibodies.Protein science : a publication of the Protein Society · 2024Article
- Infliximab Limits Injury in Myocardial Infarction.Journal of the American Heart Association · 2024Article
- 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
- Therapeutic Antibodies in Medicine.Molecules (Basel, Switzerland) · 2023Review
- Membrane Protein Binding Interactions Studied in Live Cells via Diethylpyrocarbonate Covalent Labeling Mass Spectrometry.Analytical chemistry · 2023Article
- Psoriatic arthritis: review of potential biomarkers predicting response to TNF inhibitors.Inflammopharmacology · 2023Review
- Inflammatory bowel disease biomarkers.Medicinal research reviews · 2022Review
- Complementary Structural Information for Antibody-Antigen Complexes from Hydrogen-Deuterium Exchange and Covalent Labeling Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAlthough infliximab has high efficacy in treating TNFα-associated diseases, the epitope on TNFα remains unclear.
resultsThe crystal structure of the TNFα in complex with the infliximab Fab is reported at a resolution of 2.6 Å.
conclusionTNFα E-F loop plays a crucial role in the interaction. SIGNIFICANCE: The structure may lead to understanding the mechanism of mAb anti-TNFα Monoclonal antibody (mAb) drugs have been widely used for treating tumor necrosis factor α (TNFα)-related diseases for over 10 years. Although their action has been hypothesized to depend in part on their ability to bind precursor cell surface TNFα, the precise mechanism and the epitope bound on TNFα remain unclear. In the present work, we report the crystal structure of the infliximab Fab fragment in complex with TNFα at a resolution of 2.6 Å. The key features of the TNFα E-F loop region in this complex distinguish the interaction between infliximab and TNFα from other TNF-receptor structures, revealing the mechanism of TNFα inhibition by overlapping with the TNFα-receptor interface and indicating the crucial role of the E-F loop in the action of this therapeutic antibody. This structure also indicates the formation of an aggregated network for the activation of complement-dependent cytolysis and antibody-dependent cell-mediated cytotoxicity, which result in development of granulomatous infections through TNFα blockage. These results provide the first experimental model for the interaction of TNFα with therapeutic antibodies and offer useful information for antibody optimization by understanding the precise molecular mechanism of TNFα inhibition.
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