@article{mbs:/content/journal/jgv/10.1099/0022-1317-83-3-545, author = "Alcamí, Antonio and Smith, Geoffrey L.", title = "The vaccinia virus soluble interferon-γ receptor is a homodimer", journal= "Journal of General Virology", year = "2002", volume = "83", number = "3", pages = "545-549", doi = "https://doi.org/10.1099/0022-1317-83-3-545", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-83-3-545", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", 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.", }