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Here we present the crystal structure at 1.5 \u00c5 of the immunosuppressive C-terminal portion of Lassa virus NP and illustrate that, unexpectedly, its 3D fold closely mimics that of the DEDDh family of exonucleases. Accompanying biochemical experiments illustrate that NP indeed has a previously unknown, bona fide exonuclease activity, with strict specificity for double-stranded RNA substrates. We further demonstrate that this exonuclease activity is essential for the ability of NP to suppress translocation of IFN regulatory factor 3 and block activation of the innate immune system. Thus, the nucleoprotein is a viral exonuclease with anti-immune activity, and this work provides a unique opportunity to combat arenaviral infections.<\/jats:p>","DOI":"10.1073\/pnas.1016404108","type":"journal-article","created":{"date-parts":[[2011,1,25]],"date-time":"2011-01-25T01:09:22Z","timestamp":1295917762000},"page":"2396-2401","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":265,"title":["Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3\u2032 to 5\u2032 exonuclease activity essential for immune suppression"],"prefix":"10.1073","volume":"108","author":[{"given":"Kathryn M.","family":"Hastie","sequence":"first","affiliation":[{"name":"Departments of aImmunology and Microbial Science and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christopher R.","family":"Kimberlin","sequence":"additional","affiliation":[{"name":"Departments of aImmunology and Microbial Science and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle A.","family":"Zandonatti","sequence":"additional","affiliation":[{"name":"Departments of aImmunology and Microbial Science and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian J.","family":"MacRae","sequence":"additional","affiliation":[{"name":"Molecular Biology, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Erica Ollmann","family":"Saphire","sequence":"additional","affiliation":[{"name":"Departments of aImmunology and Microbial Science and"},{"name":"The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2011,1,24]]},"reference":[{"key":"e_1_3_4_1_2","first-page":"1791","volume-title":"Fields Virology","author":"Buchmeier MJ","year":"2007","unstructured":"MJ Buchmeier, JC de la Torre, CJ Peters, Arenaviridae: The viruses and their replication. 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Am J Obstet Gynecol 194, 1532\u20131536 (2006).","journal-title":"Am J Obstet Gynecol"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"3882","DOI":"10.1128\/JVI.77.6.3882-3887.2003","article-title":"Role of the virus nucleoprotein in the regulation of lymphocytic choriomeningitis virus transcription and RNA replication","volume":"77","author":"Pinschewer DD","year":"2003","unstructured":"DD Pinschewer, M Perez, JC de la Torre, Role of the virus nucleoprotein in the regulation of lymphocytic choriomeningitis virus transcription and RNA replication. J Virol 77, 3882\u20133887 (2003).","journal-title":"J Virol"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/j.virusres.2003.11.017","article-title":"Characterization of the Lassa virus matrix protein Z: Electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP)","volume":"100","author":"Eichler R","year":"2004","unstructured":"R Eichler, et al., Characterization of the Lassa virus matrix protein Z: Electron microscopic study of virus-like particles and interaction with the nucleoprotein (NP). Virus Res 100, 249\u2013255 (2004).","journal-title":"Virus Res"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"3603","DOI":"10.1128\/JVI.02429-09","article-title":"Efficient budding of the Tacaribe virus matrix protein Z requires the nucleoprotein","volume":"84","author":"Groseth A","year":"2010","unstructured":"A Groseth, S Wolff, T Strecker, T Hoenen, S Becker, Efficient budding of the Tacaribe virus matrix protein Z requires the nucleoprotein. 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Virus Res 22, 185\u2013198 (1992).","journal-title":"Virus Res"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"5415","DOI":"10.1128\/JVI.02417-09","article-title":"A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles","volume":"84","author":"Shtanko O","year":"2010","unstructured":"O Shtanko, et al., A role for the C terminus of Mopeia virus nucleoprotein in its incorporation into Z protein-induced virus-like particles. J Virol 84, 5415\u20135422 (2010).","journal-title":"J Virol"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1038\/ni1087","article-title":"The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses","volume":"5","author":"Yoneyama M","year":"2004","unstructured":"M Yoneyama, et al., The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses. 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J Virol 83, 5890\u20135903 (2009).","journal-title":"J Virol"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"6482","DOI":"10.1128\/JVI.02876-06","article-title":"Lassa virus infection in experimentally infected marmosets: Liver pathology and immunophenotypic alterations in target tissues","volume":"81","author":"Carrion R","year":"2007","unstructured":"R Carrion, et al., Lassa virus infection in experimentally infected marmosets: Liver pathology and immunophenotypic alterations in target tissues. J Virol 81, 6482\u20136490 (2007).","journal-title":"J Virol"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"7960","DOI":"10.1128\/JVI.00536-07","article-title":"Early blood profiles of virus infection in a monkey model for Lassa fever","volume":"81","author":"Djavani MM","year":"2007","unstructured":"MM Djavani, et al., Early blood profiles of virus infection in a monkey model for Lassa fever. 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J Virol 80, 9192\u20139199 (2006).","journal-title":"J Virol"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"11330","DOI":"10.1128\/JVI.00763-09","article-title":"Identification of amino acid residues critical for the anti-interferon activity of the nucleoprotein of the prototypic arenavirus lymphocytic choriomeningitis virus","volume":"83","author":"Mart\u00ednez-Sobrido L","year":"2009","unstructured":"L Mart\u00ednez-Sobrido, et al., Identification of amino acid residues critical for the anti-interferon activity of the nucleoprotein of the prototypic arenavirus lymphocytic choriomeningitis virus. J Virol 83, 11330\u201311340 (2009).","journal-title":"J Virol"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1126\/science.1925561","article-title":"Determination of macromolecular structures from anomalous diffraction of synchrotron radiation","volume":"254","author":"Hendrickson WA","year":"1991","unstructured":"WA Hendrickson, Determination of macromolecular structures from anomalous diffraction of synchrotron radiation. Science 254, 51\u201358 (1991).","journal-title":"Science"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0022-2836(05)80360-2","article-title":"Basic local alignment search tool","volume":"215","author":"Altschul SF","year":"1990","unstructured":"SF Altschul, W Gish, W Miller, EW Myers, DJ Lipman, Basic local alignment search tool. J Mol Biol 215, 403\u2013410 (1990).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1093\/bioinformatics\/bti125","article-title":"Protein homology detection by HMM\u2013HMM comparison","volume":"21","author":"S\u00f6ding J","year":"2005","unstructured":"J S\u00f6ding, Protein homology detection by HMM\u2013HMM comparison. Bioinformatics 21, 951\u2013960 (2005).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1093\/bioinformatics\/16.6.566","article-title":"DaliLite workbench for protein structure comparison","volume":"16","author":"Holm L","year":"2000","unstructured":"L Holm, J Park, DaliLite workbench for protein structure comparison. Bioinformatics 16, 566\u2013567 (2000).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1093\/nar\/29.5.1017","article-title":"Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution","volume":"29","author":"Zuo Y","year":"2001","unstructured":"Y Zuo, MP Deutscher, Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution. Nucleic Acids Res 29, 1017\u20131026 (2001).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.febslet.2004.09.074","article-title":"Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease","volume":"577","author":"Horio T","year":"2004","unstructured":"T Horio, et al., Crystal structure of human ISG20, an interferon-induced antiviral ribonuclease. FEBS Lett 577, 111\u2013116 (2004).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/S0969-2126(02)00738-4","article-title":"Structural basis for proofreading during replication of the Escherichia coli chromosome","volume":"10","author":"Hamdan S","year":"2002","unstructured":"S Hamdan, PD Carr, SE Brown, DL Ollis, NE Dixon, Structural basis for proofreading during replication of the Escherichia coli chromosome. Structure 10, 535\u2013546 (2002).","journal-title":"Structure"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"6498","DOI":"10.1073\/pnas.90.14.6498","article-title":"A general two-metal-ion mechanism for catalytic RNA","volume":"90","author":"Steitz TA","year":"1993","unstructured":"TA Steitz, JA Steitz, A general two-metal-ion mechanism for catalytic RNA. Proc Natl Acad Sci USA 90, 6498\u20136502 (1993).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1021\/bi981537g","article-title":"Structures of normal single-stranded DNA and deoxyribo-3\u2032-S-phosphorothiolates bound to the 3\u2032-5\u2032 exonucleolytic active site of DNA polymerase I from Escherichia coli","volume":"38","author":"Brautigam CA","year":"1999","unstructured":"CA Brautigam, S Sun, JA Piccirilli, TA Steitz, Structures of normal single-stranded DNA and deoxyribo-3\u2032-S-phosphorothiolates bound to the 3\u2032-5\u2032 exonucleolytic active site of DNA polymerase I from Escherichia coli. Biochemistry 38, 696\u2013704 (1999).","journal-title":"Biochemistry"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.str.2005.04.015","article-title":"Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing","volume":"13","author":"Zuo Y","year":"2005","unstructured":"Y Zuo, Y Wang, A Malhotra, Crystal structure of Escherichia coli RNase D, an exoribonuclease involved in structured RNA processing. Structure 13, 973\u2013984 (2005).","journal-title":"Structure"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1002\/j.1460-2075.1991.tb07917.x","article-title":"Structural basis for the 3\u2032-5\u2032 exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism","volume":"10","author":"Beese LS","year":"1991","unstructured":"LS Beese, TA Steitz, Structural basis for the 3\u2032-5\u2032 exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism. EMBO J 10, 25\u201333 (1991).","journal-title":"EMBO J"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1038\/81978","article-title":"Structure of Escherichia coli exonuclease I suggests how processivity is achieved","volume":"7","author":"Breyer WA","year":"2000","unstructured":"WA Breyer, BW Matthews, Structure of Escherichia coli exonuclease I suggests how processivity is achieved. Nat Struct Biol 7, 1125\u20131128 (2000).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"6196","DOI":"10.1128\/jvi.64.12.6196-6203.1990","article-title":"A novel mechanism for the initiation of Tacaribe arenavirus genome replication","volume":"64","author":"Garcin D","year":"1990","unstructured":"D Garcin, D Kolakofsky, A novel mechanism for the initiation of Tacaribe arenavirus genome replication. J Virol 64, 6196\u20136203 (1990).","journal-title":"J Virol"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1126\/science.8469987","article-title":"Structure of DNA polymerase I Klenow fragment bound to duplex DNA","volume":"260","author":"Beese LS","year":"1993","unstructured":"LS Beese, V Derbyshire, TA Steitz, Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science 260, 352\u2013355 (1993).","journal-title":"Science"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"448","DOI":"10.1128\/MCB.01006-08","article-title":"Crystal structure of CRN-4: Implications for domain function in apoptotic DNA degradation","volume":"29","author":"Hsiao YY","year":"2009","unstructured":"YY Hsiao, et al., Crystal structure of CRN-4: Implications for domain function in apoptotic DNA degradation. Mol Cell Biol 29, 448\u2013457 (2009).","journal-title":"Mol Cell Biol"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1126\/science.2832946","article-title":"Genetic and crystallographic studies of the 3\u2032,5\u2032-exonucleolytic site of DNA polymerase I","volume":"240","author":"Derbyshire V","year":"1988","unstructured":"V Derbyshire, et al., Genetic and crystallographic studies of the 3\u2032,5\u2032-exonucleolytic site of DNA polymerase I. Science 240, 199\u2013201 (1988).","journal-title":"Science"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"7067","DOI":"10.1016\/S0021-9258(18)88888-3","article-title":"Purification and characterization of Escherichia coli RNase T","volume":"260","author":"Deutscher MP","year":"1985","unstructured":"MP Deutscher, CW Marlor, Purification and characterization of Escherichia coli RNase T. J Biol Chem 260, 7067\u20137071 (1985).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1056\/NEJMoa053240","article-title":"Transmission of lymphocytic choriomeningitis virus by organ transplantation","volume":"354","author":"Fischer SA","year":"2006","unstructured":"SA Fischer, et al., Transmission of lymphocytic choriomeningitis virus by organ transplantation. N Engl J Med 354, 2235\u20132249 (2006).","journal-title":"N Engl J Med"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"5108","DOI":"10.1073\/pnas.0508200103","article-title":"Discovery of an RNA virus 3\u2032->5\u2032 exoribonuclease that is critically involved in coronavirus RNA synthesis","volume":"107","author":"Minskaia E","year":"2006","unstructured":"E Minskaia, et al., Discovery of an RNA virus 3\u2032->5\u2032 exoribonuclease that is critically involved in coronavirus RNA synthesis. Proc Natl Acad Sci USA 107, 5108\u20135113 (2006).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"e1000896","DOI":"10.1371\/journal.ppat.1000896","article-title":"Infidelity of SARS-CoV Nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing","volume":"6","author":"Eckerle LD","year":"2010","unstructured":"LD Eckerle, et al., Infidelity of SARS-CoV Nsp14-exonuclease mutant virus replication is revealed by complete genome sequencing. PLoS Pathog 6, e1000896 (2010).","journal-title":"PLoS Pathog"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1038\/ni.1941","article-title":"The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1","volume":"11","author":"Yan N","year":"2010","unstructured":"N Yan, AD Regalado-Magdos, B Stiggelbout, MA Lee-Kirsch, J Lieberman, The cytosolic exonuclease TREX1 inhibits the innate immune response to human immunodeficiency virus type 1. Nat Immunol 11, 1005\u20131013 (2010).","journal-title":"Nat Immunol"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1073\/pnas.0910547107","article-title":"Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression","volume":"107","author":"Kimberlin CR","year":"2010","unstructured":"CR Kimberlin, et al., Ebolavirus VP35 uses a bimodal strategy to bind dsRNA for innate immune suppression. Proc Natl Acad Sci USA 107, 314\u2013319 (2010).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/nsmb.1765","article-title":"Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35","volume":"17","author":"Leung DW","year":"2010","unstructured":"DW Leung, et al., Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35. Nat Struct Mol Biol 17, 165\u2013172 (2010).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"1718","DOI":"10.1107\/S090744499900935X","article-title":"The finer things in X-ray diffraction data collection","volume":"55","author":"Pflugrath JW","year":"1999","unstructured":"JW Pflugrath, The finer things in X-ray diffraction data collection. 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Acta Crystallogr D Biol Crystallogr 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: Application to microtubules and the ribosome","volume":"98","author":"Baker NA","year":"2001","unstructured":"NA Baker, D Sept, S Joseph, MJ Holst, JA McCammon, Electrostatics of nanosystems: Application to microtubules and the ribosome. Proc Natl Acad Sci USA 98, 10037\u201310041 (2001).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1038\/nature09605","article-title":"Cap binding and immune evasion revealed by Lassa nucleoprotein structure","volume":"468","author":"Qi X","year":"2010","unstructured":"X Qi, et al., Cap binding and immune evasion revealed by Lassa nucleoprotein structure. 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