Abstract
The vaccinia virus (VV) interferon (IFN)-gamma receptor (IFN-gammaR) is a 43 kDa soluble glycoprotein that is secreted from infected cells early during infection. Here we demonstrate that the IFN-gammaR from VV, cowpox virus and camelpox virus exists naturally as a homodimer, whereas the cellular IFN-gammaR dimerizes only upon binding the homodimeric IFN-gamma. 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-gamma in solution.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Camelus / virology
-
Cell Line
-
Cowpox virus / chemistry
-
Cross-Linking Reagents / metabolism
-
Dimerization
-
Disulfides / metabolism
-
Humans
-
Interferon gamma Receptor
-
Interferon-gamma / metabolism
-
Molecular Weight
-
Protein Binding
-
Protein Structure, Quaternary
-
Protein Subunits
-
Receptors, Interferon / chemistry*
-
Receptors, Interferon / metabolism*
-
Recombinant Proteins
-
Solubility
-
Solutions
-
Vaccinia virus / chemistry*
-
Viral Proteins / chemistry*
-
Viral Proteins / metabolism*
Substances
-
Cross-Linking Reagents
-
Disulfides
-
Protein Subunits
-
Receptors, Interferon
-
Recombinant Proteins
-
Solutions
-
Viral Proteins
-
Interferon-gamma