@article{mbs:/content/journal/jgv/10.1099/0022-1317-72-1-67, author = "Walker, Peter J. and Byrne, Keren A. and Cybinski, Daisy H. and Doolan, Denise L. and Wang, Yonghong", title = "Proteins of Bovine Ephemeral Fever Virus", journal= "Journal of General Virology", year = "1991", volume = "72", number = "1", pages = "67-74", doi = "https://doi.org/10.1099/0022-1317-72-1-67", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-72-1-67", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The proteins of bovine ephemeral fever virus (BEFV) were examined in purified virions and in infected BHK-21 cells. Five structural proteins were named L (180K), G (81K), N (52K), M1 (43K) and M2 (29K). The 81 K G protein incorporated [3H]glucosamine, was removed from virions by treatment with Triton X-100 and bound monoclonal antibodies which were both neutralizing and protective. Treatment of virions with Triton X-100 and 0.2 to 1.0 m-NaCl progressively released L, M1 and M2. The N protein remained associated with nucleocapsids in up to 2.5 m-NaCl. The glycoprotein (G), nucleoprotein (N) and matrix protein (M2) were phosphorylated. In BEFV-infected BHK-21 cells, five virus-induced proteins were detected from 12 h post-infection. The L, N, M1 and M2 proteins corresponded to those detected in virions whereas the G protein existed in two forms. In tunicamycin-treated cells these occurred as 67K and 71K non-glycosylated precursors. In the absence of tunicamycin, 77K and 79K glycosylated forms were further modified to produce the 81K virion G protein and a 90K cell-associated form. Five viral proteins were also detected in cells infected with the closely related Berrimah virus; the Berrimah virus G protein was also present in two forms.", }