1887

Abstract

The vaccinia virus (VV) interferon (IFN)-γ receptor (IFN-γR) is a 43 kDa soluble glycoprotein that is secreted from infected cells early during infection. Here we demonstrate that the IFN-γR from VV, cowpox virus and camelpox virus exists naturally as a homodimer, whereas the cellular IFN-γR dimerizes only upon binding the homodimeric IFN-γ. The existence of the virus protein as a dimer in the absence of ligand may provide an advantage to the virus in efficient binding and inhibition of IFN-γ in solution.

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2002-03-01
2021-01-19
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