ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 80 citations in OpenAlex.
- Article
- An ancient evolutionary origin for IL-1 cytokines.Nature ecology & evolution · 2026Article
- Exploration of the protein and pharmacological landscape of monkeypox virus treatment: from entry point to end point.Molecular diversity · 2026Review
- Role of Non-Binding T63 Alteration in IL-18 Binding.International journal of molecular sciences · 2024Article
- Interleukin‑18 binding protein: Biological properties and roles in human and animal immune regulation (Review).Biomedical reports · 2024Review
- Molluscum Contagiosum Virus: Biology and Immune Response.Advances in experimental medicine and biology · 2024Review
- Identification of core therapeutic targets for Monkeypox virus and repurposing potential of drugs: A WEB prediction approach.PloS one · 2024Article
- A small non-interface surface epitope in human IL18 mediates the dynamics and self-assembly of IL18-IL18BP heterodimers.Computational and structural biotechnology journal · 2023Article
- Interleukin-18 and IL-18BP in inflammatory dermatological diseases.Frontiers in immunology · 2023Review
- How to Inhibit Nuclear Factor-Kappa B Signaling: Lessons from Poxviruses.Pathogens (Basel, Switzerland) · 2022Review
- EF-hand protein, EfhP, specifically binds CaScientific reports · 2022Article
- Crystal structure of the middle and C-terminal domains of Hsp90α labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target.Acta crystallographica. Section D, Structural biology · 2022Article
- Structural basis of human IL-18 sequestration by the decoy receptor IL-18 binding protein in inflammation and tumor immunity.The Journal of biological chemistry · 2022Article
- Baseline Gene Expression Levels in Falkland-Malvinas Island Penguins: Towards a New Monitoring Paradigm.Life (Basel, Switzerland) · 2022Article
- Structure and function of an effector domain in antiviral factors and tumor suppressors SAMD9 and SAMD9L.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure of the unique tetrameric STENOFOLIA homeodomain bound with target promoter DNA.Acta crystallographica. Section D, Structural biology · 2021Article
- Molecular cloning and characterisation of chicken IL-18 binding protein.Developmental and comparative immunology · 2021Article
- Insight into the structures of Interleukin-18 systems.Computational biology and chemistry · 2020Article
- Structural Basis of IL-1 Family Cytokine Signaling.Frontiers in immunology · 2019Review
- Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Human interleukin-18 (hIL-18) is a cytokine that plays an important role in inflammation and host defense against microbes. Its activity is regulated in vivo by a naturally occurring antagonist, the human IL-18-binding protein (IL-18BP). Functional homologs of human IL-18BP are encoded by all orthopoxviruses, including variola virus, the causative agent of smallpox. They contribute to virulence by suppressing IL-18-mediated immune responses. Here, we describe the 2.0-A resolution crystal structure of an orthopoxvirus IL-18BP, ectromelia virus IL-18BP (ectvIL-18BP), in complex with hIL-18. The hIL-18 structure in the complex shows significant conformational change at the binding interface compared with the structure of ligand-free hIL-18, indicating that the binding is mediated by an induced-fit mechanism. EctvIL-18BP adopts a canonical Ig fold and interacts via one edge of its beta-sandwich with 3 cavities on the hIL-18 surface through extensive hydrophobic and hydrogen bonding interactions. Most of the ectvIL-18BP residues that participate in these interactions are conserved in both human and viral homologs, explaining their functional equivalence despite limited sequence homology. EctvIL-18BP blocks a putative receptor-binding site on IL-18, thus preventing IL-18 from engaging its receptor. Our structure provides insights into how IL-18BPs modulate hIL-18 activity. The revealed binding interface provides the basis for rational design of inhibitors against orthopoxvirus IL-18BP (for treating orthopoxvirus infection) or hIL-18 (for treating certain inflammatory and autoimmune diseases).
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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.