The vaccinia virus soluble interferon-gamma receptor is a homodimer

J Gen Virol. 2002 Mar;83(Pt 3):545-549. doi: 10.1099/0022-1317-83-3-545.

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