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Poxviruses encode a large number of proteins that attenuate the
inflammatory and immune responses to infection. In this report we
demonstrate that a number of orthopoxviruses express a type I
interferon (IFN)-binding protein, which is encoded by the B18R open
reading frame in the WR strain of vaccinia virus. The B18R protein has
significant regions of homology with the
Volume 270,
Number 27,
Issue of July 07, pp. 15974-15978, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Transmembrane Signaling
subunits of the mouse,
human, and bovine type I IFN receptors, bound human IFN2 with high
affinity, and inhibited transmembrane signaling as demonstrated by
inhibition of Fc receptor factor 1/
2 and
interferon-stimulated gene factor-3 formation as well as inhibition of
the IFN
antiviral response. Among viral host response modifiers,
the B18R protein is unique inasmuch as it exists as a soluble
extracellular as well as a cell surface protein and thus should
effectively block both autocrine and paracrine functions of IFN.
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