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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

A poxvirus protein that binds to and inactivates IL-18, and inhibits NK cell response.

IL-18 induces IFN-gamma and NK cell cytotoxicity, making it a logical target for viral antagonism of host defense. We demonstrate that the ectromelia poxvirus p13 protein, bearing homology to the mammalian IL-18 binding protein, binds IL-18, and inhibits its activity in vitro. Binding of IL-18 to the viral p13 protein was compared with binding to the cellular IL-18R. The dissociation constant of p13 for murine IL-18 is 5 nM, compared with 0.2 nM for the cellular receptor heterodimer. Mice infected with a p13 deletion mutant of ectromelia virus had elevated cytotoxicity for YAC-1 tumor cell targets compared with control animals. Additionally, the p13 deletion mutant virus exhibited decreased levels of infectivity. Our data suggest that inactivation of IL-18, and subsequent impairment of NK cell cytotoxicity, may be one mechanism by which ectromelia evades the host immune response.[1]


  1. A poxvirus protein that binds to and inactivates IL-18, and inhibits NK cell response. Born, T.L., Morrison, L.A., Esteban, D.J., VandenBos, T., Thebeau, L.G., Chen, N., Spriggs, M.K., Sims, J.E., Buller, R.M. J. Immunol. (2000) [Pubmed]
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