Abstract
The soluble vaccinia virus-encoded protein B18R inhibits the antiviral activity and cellular binding of the type I interferons (IFN)-alpha, - beta and -omega of different mammalian species. Recently, a novel type I IFN was detected in pigs and classified as a member of a distinct IFN family designated IFN-delta. Our study aimed to determine if the structural properties of this shortest (149 residues long) type I IFN allow its interaction with the type I IFN-binding protein B18R. Experiments using bovine (MDBK) cells demonstrated that B18R neutralized the antiviral activity of porcine IFN-delta with high efficiency. Preincubation of B18R with radiolabelled IFN-delta specifically inhibited binding of IFN to bovine cells. These data indicate that the overall conformation of the novel IFN-delta might be similar to that of other type I IFNs.