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Animal: DNA Viruses |
receptor and its contribution to virus virulence
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK1
Author for correspondence: Geoffrey Smith. Present address: Department of Virology, The Wright–Fleming Institute, Faculty of Medicine, Imperial College, St Mary’s Campus, Norfolk Place, London W2 1PG, UK. Fax +44 207 594 3973. e-mail glsmith{at}ic.ac.uk
Vaccinia virus (VV) strain Western Reserve gene B8R encodes a 43 kDa glycoprotein that is secreted from infected cells early in infection as a homodimer. This protein has amino acid similarity with the extracellular domain of cellular IFN-
receptor (IFN-R) and binds and inhibits IFN- from a wide range of species. Here we demonstrate that the B8R protein also inhibits equine IFN-. The 5' end of the B8R mRNA has been mapped by primer extension analysis and the contribution of IFN-Rs to VV virulence was studied by the construction of a deletion mutant lacking the B8R gene (v
B8R) and a revertant virus (vB8R-R) in which the B8R gene was re-inserted into the deletion mutant. A recombinant virus that expressed a soluble form of the mouse IFN-R was also constructed and studied. The virulence of these viruses was tested in rodent models of infection. In mice, the loss of the VV IFN-R did not affect virulence compared with WT and revertant viruses, consistent with the low affinity of the VV IFN-R for mouse IFN-. However, expression of the mouse soluble IFN-R increased virus virulence slightly. In rabbit skin, loss of the VV IFN-R produced lesions with histological differences compared with WT and revertant viruses. Lastly, the affinity constants of the VV IFN-R for human and mouse IFN- were determined by surface plasmon resonance.
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