%0 Journal Article %A Ohta, K. %A Goto, H. %A Yumine, N. %A Nishio, M. %T Human parainfluenza virus type 2 V protein inhibits and antagonizes tetherin %D 2016 %J Journal of General Virology, %V 97 %N 3 %P 561-570 %@ 1465-2099 %R https://doi.org/10.1099/jgv.0.000373 %I Microbiology Society, %X Tetherin (BST-2/CD317/HM1.24) is an antiviral membrane protein that prevents the release of enveloped viruses from the cell surface. We found that the growth of human parainfluenza virus type 2 (hPIV-2), but not that of V protein-deficient recombinant hPIV-2, was inhibited by tetherin. V protein immunoprecipitates with tetherin, and this interaction requires its C-terminal Trp residues. The glycosyl phosphatidylinositol attachment signal of tetherin, but not its cytoplasmic tail, was necessary for its binding with V. The distribution of the V protein clearly changed when co-expressed with tetherin in plasmid-transfected cells. hPIV-2 infection of HeLa cells reduced cell surface tetherin without affecting total cellular tetherin. This reduction also occurred in HeLa cells constitutively expressing V, whereas mutated V protein did not affect the cell surface tetherin. Our results suggest that hPIV-2 V protein antagonizes tetherin by binding it and reducing its presence at the cell surface. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/jgv.0.000373