{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T06:04:58Z","timestamp":1792735498190,"version":"4.5.0"},"reference-count":32,"publisher":"National Academy of Sciences","issue":"49","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2004,12,7]]},"abstract":"<jats:p>\n                    Most paramyxoviruses circumvent the IFN response by blocking IFN signaling and limiting the production of IFN by virus-infected cells. Here we report that the highly conserved cysteine-rich C-terminal domain of the V proteins of a wide variety of paramyxoviruses binds melanoma differentiation-associated gene 5 (mda-5) product. mda-5 is an IFN-inducible host cell DExD\/H box helicase that contains a caspase recruitment domain at its N terminus. Overexpression of mda-5 stimulated the basal activity of the\n                    <jats:italic>IFN-<\/jats:italic>\n                    \u03b2 promoter in reporter gene assays and significantly enhanced the activation of the\n                    <jats:italic>IFN-<\/jats:italic>\n                    \u03b2 promoter by intracellular dsRNA. Both these activities were repressed by coexpression of the V proteins of simian virus 5, human parainfluenza virus 2, mumps virus, Sendai virus, and Hendra virus. Similar results to the reporter assays were obtained by measuring IFN production. Inhibition of mda-5 by RNA interference or by dominant interfering forms of mda-5 significantly inhibited the activation of the\n                    <jats:italic>IFN-<\/jats:italic>\n                    \u03b2 promoter by dsRNA. It thus appears that mda-5 plays a central role in an intracellular signal transduction pathway that can lead to the activation of the\n                    <jats:italic>IFN-<\/jats:italic>\n                    \u03b2 promoter, and that the V proteins of paramyxoviruses interact with mda-5 to block its activity.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0407639101","type":"journal-article","created":{"date-parts":[[2004,11,24]],"date-time":"2004-11-24T20:24:43Z","timestamp":1101327883000},"page":"17264-17269","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":870,"title":["The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the\n                    <i>IFN<\/i>\n                    -\u03b2 promoter"],"prefix":"10.1073","volume":"101","author":[{"given":"J.","family":"Andrejeva","sequence":"first","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"K. S.","family":"Childs","sequence":"additional","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D. F.","family":"Young","sequence":"additional","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"T. S.","family":"Carlos","sequence":"additional","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N.","family":"Stock","sequence":"additional","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"S.","family":"Goodbourn","sequence":"additional","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. E.","family":"Randall","sequence":"additional","affiliation":[{"name":"School of Biology, Biomolecular Sciences Building, North Haugh, University of St. Andrews, Fife KY16 9TS, United Kingdom; and Biochemistry and Immunology, Department of Basic Medical Sciences, St. George's Hospital Medical School, University of London, London SW17 0RE, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2004,11,24]]},"reference":[{"key":"e_1_3_2_1_2","first-page":"1305","volume":"1","year":"2001","unstructured":"Lamb, R. A. & Kolakofsky, D. (2001) in Fields' Virology, eds. Fields, B. N., Knipe, D. M., Howley, P. M. & Griffin, D. E. (Lippincott Williams & Wilkins, Philadelphia), Vol. 1, pp. 1305\u20131340.","journal-title":"Fields' Virology"},{"key":"e_1_3_2_2_2","first-page":"52","volume":"3","year":"2001","unstructured":"Wang, L.-F. & Eaton, B. (2001) Infect. Dis. Rev. 3, 52\u201369.","journal-title":"Infect. Dis. 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