Orthopoxvirus Il-18 binding proteins: Affinities and antagonist activities

Silvio Calderara; Yan Xiang; Bernard Moss

doi:10.1006/viro.2000.0689

Orthopoxvirus Il-18 binding proteins: Affinities and antagonist activities

Silvio Calderara, Yan Xiang, Bernard Moss

Research output: Contribution to journal › Article › peer-review

63 Scopus citations

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-γ by murine and human IL-18. The relative affinities of the orthopoxvirus IL-18BPs are consistent with the rodent host range of the viruses.

Original language	English (US)
Pages (from-to)	22-26
Number of pages	5
Journal	Virology
Volume	279
Issue number	1
DOIs	https://doi.org/10.1006/viro.2000.0689
State	Published - 2001
Externally published	Yes

ASJC Scopus subject areas

Virology

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10.1006/viro.2000.0689

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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-γ by murine and human IL-18. The relative affinities of the orthopoxvirus IL-18BPs are consistent with the rodent host range of the viruses.",

author = "Silvio Calderara and Yan Xiang and Bernard Moss",

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doi = "10.1006/viro.2000.0689",

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AB - 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-γ by murine and human IL-18. The relative affinities of the orthopoxvirus IL-18BPs are consistent with the rodent host range of the viruses.

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Orthopoxvirus Il-18 binding proteins: Affinities and antagonist activities

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