@article{mbs:/content/journal/jgv/10.1099/0022-1317-79-7-1647, author = "Vančová, Iveta and La Bonnardiere, Claude and Kontsek, Peter", title = "Vaccinia virus protein B18R inhibits the activity and cellular binding of the novel type interferon-delta.", journal= "Journal of General Virology", year = "1998", volume = "79", number = "7", pages = "1647-1649", doi = "https://doi.org/10.1099/0022-1317-79-7-1647", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-79-7-1647", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The soluble vaccinia virus-encoded protein B18R inhibits the antiviral activity and cellular binding of the type I interferons (IFN)-α, - β and -ω of different mammalian species. Recently, a novel type IIFN was detected in pigs and classified as a member of a distinct IFN family designated IFN-λ. 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-λ with high efficiency. Preincubation of B18R with radiolabelled IFN-λ specifically inhibited binding of IFN to bovine cells. These data indicate that the overall conformation of the novel IFN-λ might be similar to that of other type I IFNs.", }