{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T04:29:27Z","timestamp":1791174567383,"version":"4.1.0"},"reference-count":28,"publisher":"National Academy of Sciences","issue":"22","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2013,5,28]]},"abstract":"<jats:p>\n                    Bunyamwera virus (BUNV), which belongs to the genus\n                    <jats:italic>Orthobunyavirus<\/jats:italic>\n                    , is the prototypical virus of the\n                    <jats:italic>Bunyaviridae<\/jats:italic>\n                    family. Similar to other negative-sense single-stranded RNA viruses, bunyaviruses possess a nucleocapsid protein (NP) to facilitate genomic RNA encapsidation and virus replication. The structures of two NPs of members of different genera within the\n                    <jats:italic>Bunyaviridae<\/jats:italic>\n                    family have been reported. However, their structures, RNA-binding features, and functions beyond RNA binding significantly differ from one another. Here, we report the crystal structure of the BUNV NP\u2013RNA complex. The polypeptide of the BUNV NP was found to possess a distinct fold among viral NPs. An N-terminal arm and a C-terminal tail were found to interact with neighboring NP protomers to form a tetrameric ring-shaped organization. Each protomer bound a 10-nt RNA molecule, which was acquired from the expression host, in the positively charged crevice between the N and C lobes. Inhomogeneous oligomerization was observed for the recombinant BUNV NP\u2013RNA complex, which was similar to the Rift Valley fever virus NP\u2013RNA complex. This result suggested that the flexibility of one NP protomer with adjacent protomers underlies the BUNV ribonucleoprotein complex (RNP) formation. Electron microscopy revealed that the monomer-sized NP\u2013RNA complex was the building block of the natural BUNV RNP. Combined with previous results indicating that mutagenesis of the interprotomer or protein\u2013RNA interface affects BUNV replication, our structure provides a great potential for understanding the mechanism underlying negative-sense single-stranded RNA RNP formation and enables the development of antiviral therapies targeting BUNV RNP formation.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1222552110","type":"journal-article","created":{"date-parts":[[2013,4,8]],"date-time":"2013-04-08T21:18:31Z","timestamp":1365455911000},"page":"9048-9053","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":59,"title":["Bunyamwera virus possesses a distinct nucleocapsid protein to facilitate genome encapsidation"],"prefix":"10.1073","volume":"110","author":[{"given":"Baobin","family":"Li","sequence":"first","affiliation":[{"name":"Laboratory of Structural Biology, School of Medicine,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Quan","family":"Wang","sequence":"additional","affiliation":[{"name":"College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xijiang","family":"Pan","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabel","family":"Fern\u00e1ndez de Castro","sequence":"additional","affiliation":[{"name":"Cell Structure Laboratory, Centro Nacional de Biotecnolog\u00eda, Consejo Superior de Investigaciones Cient\u00edficas, Cantoblanco, 28049 Madrid, Spain;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuna","family":"Sun","sequence":"additional","affiliation":[{"name":"National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Guo","sequence":"additional","affiliation":[{"name":"College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinwei","family":"Tao","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, School of Medicine,"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cristina","family":"Risco","sequence":"additional","affiliation":[{"name":"Cell Structure Laboratory, Centro Nacional de Biotecnolog\u00eda, Consejo Superior de Investigaciones Cient\u00edficas, Cantoblanco, 28049 Madrid, Spain;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sen-Fang","family":"Sui","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhiyong","family":"Lou","sequence":"additional","affiliation":[{"name":"Laboratory of Structural Biology, School of Medicine,"},{"name":"Ministry of Education Laboratory of Protein Science, and"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2013,4,8]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"5046","DOI":"10.1073\/pnas.1200808109","article-title":"Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses","volume":"109","author":"Guo Y","year":"2012","unstructured":"Y Guo, et al., Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses. 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J Gen Virol 71, 501\u2013522 (1990).","journal-title":"J Gen Virol"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1128\/JCM.01319-11","article-title":"Preparation and evaluation of recombinant severe fever with thrombocytopenia syndrome virus nucleocapsid protein for detection of total antibodies in human and animal sera by double-antigen sandwich enzyme-linked immunosorbent assay","volume":"50","author":"Jiao Y","year":"2012","unstructured":"Y Jiao, et al., Preparation and evaluation of recombinant severe fever with thrombocytopenia syndrome virus nucleocapsid protein for detection of total antibodies in human and animal sera by double-antigen sandwich enzyme-linked immunosorbent assay. 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