@article{mbs:/content/journal/jgv/10.1099/vir.0.022897-0, author = "Johns, Helen L. and Doceul, Virginie and Everett, Helen and Crooke, Helen and Charleston, Bryan and Seago, Julian", title = "The classical swine fever virus N-terminal protease Npro binds to cellular HAX-1", journal= "Journal of General Virology", year = "2010", volume = "91", number = "11", pages = "2677-2686", doi = "https://doi.org/10.1099/vir.0.022897-0", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.022897-0", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The positive-stranded RNA genome of classical swine fever virus (CSFV) encodes 12 known proteins. The first protein to be translated is the N-terminal protease (Npro). Npro helps evade the innate interferon response by targeting interferon regulatory factor-3 for proteasomal degradation and also participates in the evasion of dsRNA-induced apoptosis. To elucidate the mechanisms by which Npro functions, we performed a yeast two-hybrid screen in which the anti-apoptotic protein HAX-1 was identified. The Npro–HAX-1 interaction was confirmed using co-precipitation assays. A dramatic redistribution of both Npro and HAX-1 was observed in co-transfected cells, as well as in transfected cells infected with wild-type CSFV, but not in cells infected with an Npro-deleted CSFV strain.", }