ArticlePLoS pathogens2012
A unique bivalent binding and inhibition mechanism by the yatapoxvirus interleukin 18 binding protein.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- 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
- 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 Binding Protein in Immune Regulation and Autoimmune Diseases.Biomedicines · 2022Review
- 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
- Molecular cloning and characterisation of chicken IL-18 binding protein.Developmental and comparative immunology · 2021Article
- Complete genome sequence of a novel sea otterpox virus.Virus genes · 2018Article
- New insights into the immunomodulatory properties of poxvirus cytokine decoy receptors at the cell surface.F1000Research · 2018Review
- Identification of small molecule inhibitors of Interleukin-18.Scientific reports · 2017Article
- Mechanisms of immunomodulation by mammalian and viral decoy receptors: insights from structures.Nature reviews. Immunology · 2017Review
- Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses.Nature reviews. Microbiology · 2016Review
- The structure of a prophenoloxidase (PPO) from Anopheles gambiae provides new insights into the mechanism of PPO activation.BMC biology · 2016Article
- Crystallization of interleukin-18 for structure-based inhibitor design.Acta crystallographica. Section F, Structural biology communications · 2015Article
- The structural basis for receptor recognition of human interleukin-18.Nature communications · 2014Article
- The complete genome sequences of poxviruses isolated from a penguin and a pigeon in South Africa and comparison to other sequenced avipoxviruses.BMC genomics · 2014Article
- Structural biology of the IL-1 superfamily: key cytokines in the regulation of immune and inflammatory responses.Protein science : a publication of the Protein Society · 2014Review
- IL-18 in inflammatory and autoimmune disease.Cellular and molecular life sciences : CMLS · 2013Review
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Interleukin 18 (IL18) is a cytokine that plays an important role in inflammation as well as host defense against microbes. Mammals encode a soluble inhibitor of IL18 termed IL18 binding protein (IL18BP) that modulates IL18 activity through a negative feedback mechanism. Many poxviruses encode homologous IL18BPs, which contribute to virulence. Previous structural and functional studies on IL18 and IL18BPs revealed an essential binding hot spot involving a lysine on IL18 and two aromatic residues on IL18BPs. The aromatic residues are conserved among the very diverse mammalian and poxviruses IL18BPs with the notable exception of yatapoxvirus IL18BPs, which lack a critical phenylalanine residue. To understand the mechanism by which yatapoxvirus IL18BPs neutralize IL18, we solved the crystal structure of the Yaba-Like Disease Virus (YLDV) IL18BP and IL18 complex at 1.75 Å resolution. YLDV-IL18BP forms a disulfide bonded homo-dimer engaging IL18 in a 2∶2 stoichiometry, in contrast to the 1∶1 complex of ectromelia virus (ECTV) IL18BP and IL18. Disruption of the dimer interface resulted in a functional monomer, however with a 3-fold decrease in binding affinity. The overall architecture of the YLDV-IL18BP:IL18 complex is similar to that observed in the ECTV-IL18BP:IL18 complex, despite lacking the critical lysine-phenylalanine interaction. Through structural and mutagenesis studies, contact residues that are unique to the YLDV-IL18BP:IL18 binding interface were identified, including Q67, P116 of YLDV-IL18BP and Y1, S105 and D110 of IL18. Overall, our studies show that YLDV-IL18BP is unique among the diverse family of mammalian and poxvirus IL-18BPs in that it uses a bivalent binding mode and a unique set of interacting residues for binding IL18. However, despite this extensive divergence, YLDV-IL18BP binds to the same surface of IL18 used by other IL18BPs, suggesting that all IL18BPs use a conserved inhibitory mechanism by blocking a putative receptor-binding site on IL18.
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