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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2015,5,12]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    Infection with the Rift Valley fever virus (RVFV) has the capacity to cause fatal hemorrhagic fever in humans. A unique characteristic of RVFV infection is the presence of nuclear filaments whose formation is linked to synthesis of the viral NSs protein. We identify a crucial interaction between a \u03a9X\n                    <jats:italic>a<\/jats:italic>\n                    V motif present in the NSs protein and the p62 subunit of the host TFIIH. This interaction is required for nuclear filament formation, NSs-dependent degradation of p62 and for virulence. This \u03a9X\n                    <jats:italic>a<\/jats:italic>\n                    V motif is also found in human proteins that bind p62 and our results are an example of how viruses incorporate simple motifs into their protein sequences to mimic human proteins and enhance their functional capabilities in host cells during infections.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1503688112","type":"journal-article","created":{"date-parts":[[2015,4,30]],"date-time":"2015-04-30T17:24:52Z","timestamp":1430414692000},"page":"6021-6026","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":40,"title":["A \u03a9X\n                    <i>a<\/i>\n                    V motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence"],"prefix":"10.1073","volume":"112","author":[{"given":"Normand","family":"Cyr","sequence":"first","affiliation":[{"name":"Department of Biochemistry and Molecular Medicine, Universit\u00e9 de Montr\u00e9al, Montr\u00e9al, QC, Canada H3C 3J7; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cynthia","family":"de la Fuente","sequence":"additional","affiliation":[{"name":"National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, VA 20110"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lauriane","family":"Lecoq","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Medicine, Universit\u00e9 de Montr\u00e9al, Montr\u00e9al, QC, Canada H3C 3J7; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irene","family":"Guendel","sequence":"additional","affiliation":[{"name":"National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, VA 20110"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Philippe R.","family":"Chabot","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Medicine, Universit\u00e9 de Montr\u00e9al, Montr\u00e9al, QC, Canada H3C 3J7; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kylene","family":"Kehn-Hall","sequence":"additional","affiliation":[{"name":"National Center for Biodefense and Infectious Diseases, School of Systems Biology, George Mason University, Manassas, VA 20110"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James G.","family":"Omichinski","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Medicine, Universit\u00e9 de Montr\u00e9al, Montr\u00e9al, QC, Canada H3C 3J7; and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2015,4,27]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/S0168-1702(02)00125-9","article-title":"Antigenic drift, antigenic shift and interferon antagonists: How bunyaviruses counteract the immune system","volume":"88","author":"Weber F","year":"2002","unstructured":"F Weber, RM Elliott, Antigenic drift, antigenic shift and interferon antagonists: How bunyaviruses counteract the immune system. 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