ArticleJournal of virology2001
Correspondence of the functional epitopes of poxvirus and human interleukin-18-binding proteins.
Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
25 citing papers in PubMed, 71 citations in OpenAlex.
- Interleukin‑18 binding protein: Biological properties and roles in human and animal immune regulation (Review).Biomedical reports · 2024Review
- Molecular and genomic characterization of a novel equine molluscum contagiosum-like virus.The Journal of general virology · 2021Article
- Molecular cloning and characterisation of chicken IL-18 binding protein.Developmental and comparative immunology · 2021Article
- Molluscum contagiosum virus MC80 sabotages MHC-I antigen presentation by targeting tapasin for ER-associated degradation.PLoS pathogens · 2019Article
- Article
- Overview of the IL-1 family in innate inflammation and acquired immunity.Immunological reviews · 2018Review
- Identification of small molecule inhibitors of Interleukin-18.Scientific reports · 2017Article
- Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses.Nature reviews. Microbiology · 2016Review
- Crystallization of interleukin-18 for structure-based inhibitor design.Acta crystallographica. Section F, Structural biology communications · 2015Article
- 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
- Interleukin-18 and IL-18 binding protein.Frontiers in immunology · 2013Review
- The inflammasome as a target of modulation by DNA viruses.Future virology · 2013Article
- Decoys and Regulatory "Receptors" of the IL-1/Toll-Like Receptor Superfamily.Frontiers in immunology · 2013Article
- A unique bivalent binding and inhibition mechanism by the yatapoxvirus interleukin 18 binding protein.PLoS pathogens · 2012Article
- Structural basis for antagonism of human interleukin 18 by poxvirus interleukin 18-binding protein.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Yaba monkey tumor virus encodes a functional inhibitor of interleukin-18.Journal of virology · 2008Article
- Historical insights into cytokines.European journal of immunology · 2007Review
- Article
- A novel isoform of pro-interleukin-18 expressed in ovarian tumors is resistant to caspase-1 and -4 processing.Oncogene · 2004Article
- The genome of canarypox virus.Journal of virology · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Molluscum contagiosum virus, a human poxvirus that causes persistent small benign skin tumors, encodes a variety of putative immune defense proteins. Three such proteins, MC51L, MC53L, and MC54L, have 20 to 35% amino acid sequence identities with human interleukin-18 (hIL-18)-binding protein (hIL-18BP), a naturally occurring antagonist of the proinflammatory cytokine IL-18. We previously demonstrated that seven amino acids within the immunoglobulin-like domain of hIL-18BP were important for high-affinity binding to hIL-18. Model building indicated that MC54L, which has been shown to bind hIL-18, contains five of the seven amino acids at corresponding positions in its immunoglobulin-like domain, the exceptions being the conservative substitution of isoleucine for a leucine and the nonconservative substitution of valine for a phenylalanine. We found that individual alanine substitutions for these six identical or highly conserved amino acids of MC54L caused changes in affinity and binding free energy for hIL-18 that were quantitatively similar to those produced by mutagenesis of hIL-18BP. Furthermore, when the nonconserved valine of MC54L was mutated to phenylalanine, making it more like hIL-18BP, its affinity for hIL-18 increased more than 10-fold. In addition, the carboxyl-terminal half of MC54L, which has no similarity with hIL-18BP, was dispensable for hIL-18 binding. Thus, despite their relatively low overall sequence identity, MC54L and hIL-18BP have similar hIL-18 binding sites and functional epitopes. On the other hand, MC51L and MC53L have nonconservative substitutions of three to six of the seven critical amino acids of hIL-18BP and neither protein bound hIL-18, suggesting that they may interact with unidentified ligands.
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