1887

Abstract

The soluble vaccinia virus-encoded protein B18R inhibits the antiviral activity and cellular binding of the type I interferons (IFN)-α, - 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.

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/content/journal/jgv/10.1099/0022-1317-79-7-1647
1998-07-01
2022-05-28
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