Reports

Crystal Structure of the Rabies Virus Nucleoprotein-RNA Complex

Aurélie A. V. Albertini,^1* Amy K. Wernimont,^2* Tadeusz Muziol,² Raimond B. G. Ravelli,² Cedric R. Clapier,² Guy Schoehn,¹ Winfried Weissenhorn,² Rob W. H. Ruigrok¹

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.

¹ Institut de Virologie Moléculaire et Structurale, FRE 2854 Université Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France.
² European Molecular Biology Laboratory (EMBL), Boite Postale 181, 38042 Grenoble, France.

Note added in proof: This version of the manuscript is slightly changed relative to the version that was published Science Express on June 15. Improved refinement of the structure led to a better definition of the following regions, which have been changed accordingly: the N terminus, including the ß hairpin leading to helix 1; Tyr¹⁶¹, Arg¹⁶⁸, and Arg⁴³⁴ contacting the RNA; as well as helices 13 to 16 of the C-terminal domain. None of the changes made influences the overall conformation of the structure or any of the conclusions drawn from the structure.

^* These authors contributed equally to this work.

To whom correspondence should be addressed. E-mail: weissen{at}embl-grenoble.fr

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