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Orthopoxvirus IL-18 binding proteins: affinities and antagonist activities.
- Source :
-
Virology [Virology] 2001 Jan 05; Vol. 279 (1), pp. 22-6. - Publication Year :
- 2001
-
Abstract
- The affinities of purified recombinant human IL-18 binding protein (BP) and ectromelia and cowpox virus homologs for human and murine IL-18 were compared by plasmon resonance. The dissociation constants of human IL-18BP were similar for murine and human IL-18. By contrast, the dissociation constants of the viral proteins for murine IL-18 were 12- to 50-fold lower than that for human IL-18. The ectromelia and cowpox virus proteins were biologically active, as judged by their ability to inhibit induction of interferon-gamma by murine and human IL-18. The relative affinities of the orthopoxvirus IL-18BPs are consistent with the rodent host range of the viruses.<br /> (Copyright 2001 Academic Press.)
- Subjects :
- Animals
Cell Line
Cowpox virus genetics
Cowpox virus metabolism
Ectromelia virus genetics
Ectromelia virus metabolism
Glycoproteins chemistry
Glycoproteins genetics
Glycoproteins pharmacology
Humans
Intercellular Signaling Peptides and Proteins
Interferon-gamma biosynthesis
Interleukin-18 antagonists & inhibitors
Interleukin-18 genetics
Interleukin-18 metabolism
Interleukin-18 pharmacology
Lipopolysaccharides pharmacology
Mice
Orthopoxvirus genetics
Poxviridae Infections virology
Recombinant Proteins metabolism
Spleen cytology
Spleen immunology
Surface Plasmon Resonance
Tumor Necrosis Factor-alpha pharmacology
Glycoproteins metabolism
Orthopoxvirus metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0042-6822
- Volume :
- 279
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Virology
- Publication Type :
- Academic Journal
- Accession number :
- 11145885
- Full Text :
- https://doi.org/10.1006/viro.2000.0689