{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:18:53Z","timestamp":1791397133315,"version":"4.3.3"},"reference-count":28,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"5785","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2006,7,21]]},"abstract":"<jats:p>Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle.<\/jats:p>","DOI":"10.1126\/science.1125280","type":"journal-article","created":{"date-parts":[[2006,6,15]],"date-time":"2006-06-15T21:06:07Z","timestamp":1150405567000},"page":"360-363","source":"Crossref","is-referenced-by-count":315,"title":["Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex"],"prefix":"10.1126","volume":"313","author":[{"given":"Aure\u0301lie A. 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G.","family":"Ravelli","sequence":"additional","affiliation":[{"name":"Institut de Virologie Mole\u0301culaire et Structurale, FRE 2854 Universite\u0301 Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France."},{"name":"European Molecular Biology Laboratory (EMBL), Boite Postale 181, 38042 Grenoble, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cedric R.","family":"Clapier","sequence":"additional","affiliation":[{"name":"Institut de Virologie Mole\u0301culaire et Structurale, FRE 2854 Universite\u0301 Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France."},{"name":"European Molecular Biology Laboratory (EMBL), Boite Postale 181, 38042 Grenoble, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guy","family":"Schoehn","sequence":"additional","affiliation":[{"name":"Institut de Virologie Mole\u0301culaire et Structurale, FRE 2854 Universite\u0301 Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France."},{"name":"European Molecular Biology Laboratory (EMBL), Boite Postale 181, 38042 Grenoble, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Winfried","family":"Weissenhorn","sequence":"additional","affiliation":[{"name":"Institut de Virologie Mole\u0301culaire et Structurale, FRE 2854 Universite\u0301 Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France."},{"name":"European Molecular Biology Laboratory (EMBL), Boite Postale 181, 38042 Grenoble, France."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rob W. 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Kolakofsky (Geneva) Y. Gaudin and D. Blondel (Gif-sur-Yvette) for many discussions and ideas; F. Iseni and M. Mavrakis for early contributions to the project; S. Cusack for discussions and comments on the text; and all members of the EMBL European Synchrotron Radiation Facility (ESRF) Joint Structural Biology Group (JSBG) for access to the ESRF beam lines. This work was supported by the EMBL (W.W.) the Deutsche Forschungsgemeinschaft SFB 593 (W.W.) the Universit\u00e9 Joseph Fourier (R.W.H.R.) the CNRS (G.S.) an EMBO fellowship (C.R.C.) and a Ph.D. fellowship from the French Ministry for Education Research and Technology (A.A.V.A.). 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