Related Content
Search Google Scholar for:
|
Published Online June 15, 2006
Science
DOI: 10.1126/science.1125280
|
|
Reports
Submitted on January 23, 2006
Accepted on May 17, 2006
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. Ruigrok 1
1 Institut de Virologie Moléculaire et Structurale, FRE 2854 Université Joseph Fourier-CNRS
2 European Molecular Biology Laboratory (EMBL), Boite Postale 181, 38042 Grenoble, France.
* To whom correspondence should be addressed.
Winfried Weissenhorn , E-mail: weissen{at}embl-grenoble.fr
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.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design.
- A. K.-L. Ng, H. Zhang, K. Tan, Z. Li, J.-h. Liu, P. K.-S. Chan, S.-M. Li, W.-Y. Chan, S. W.-N. Au, A. Joachimiak, et al. (2008)
FASEB J
22, 3638-3647
| Abstract »
| Full Text »
| PDF »
- Cellular La Protein Shields Nonsegmented Negative-Strand RNA Viral Leader RNA from RIG-I and Enhances Virus Growth by Diverse Mechanisms.
- V. Bitko, A. Musiyenko, M. A. Bayfield, R. J. Maraia, and S. Barik (2008)
J. Virol.
82, 7977-7987
| Abstract »
| Full Text »
| PDF »
- Role of Intermolecular Interactions of Vesicular Stomatitis Virus Nucleoprotein in RNA Encapsidation.
- X. Zhang, T. J. Green, J. Tsao, S. Qiu, and M. Luo (2008)
J. Virol.
82, 674-682
| Abstract »
| Full Text »
| PDF »
- Interaction of Vesicular Stomatitis Virus P and N Proteins: Identification of Two Overlapping Domains at the N Terminus of P That Are Involved in N0-P Complex Formation and Encapsidation of Viral Genome RNA.
- M. Chen, T. Ogino, and A. K. Banerjee (2007)
J. Virol.
81, 13478-13485
| Abstract »
| Full Text »
| PDF »
- Cis-acting elements in the antigenomic promoter of Nipah virus.
- P. Walpita and C. J. Peters (2007)
J. Gen. Virol.
88, 2542-2551
| Abstract »
| Full Text »
| PDF »
- RSV604, a Novel Inhibitor of Respiratory Syncytial Virus Replication.
- J. Chapman, E. Abbott, D. G. Alber, R. C. Baxter, S. K. Bithell, E. A. Henderson, M. C. Carter, P. Chambers, A. Chubb, G. S. Cockerill, et al. (2007)
Antimicrob. Agents Chemother.
51, 3346-3353
| Abstract »
| Full Text »
| PDF »
- The 24-Angstrom Structure of Respiratory Syncytial Virus Nucleocapsid Protein-RNA Decameric Rings.
- K. MacLellan, C. Loney, R. P. Yeo, and D. Bhella (2007)
J. Virol.
81, 9519-9524
| Abstract »
| Full Text »
| PDF »
- Membrane and protein dynamics in live plant nuclei infected with Sonchus yellow net virus, a plant-adapted rhabdovirus.
- M. M. Goodin, R. Chakrabarty, S. Yelton, K. Martin, A. Clark, and R. Brooks (2007)
J. Gen. Virol.
88, 1810-1820
| Abstract »
| Full Text »
| PDF »
- Sequence-specific binding of single-stranded RNA: is there a code for recognition?.
- S. D. Auweter, F. C. Oberstrass, and F. H.-T. Allain (2006)
Nucleic Acids Res.
34, 4943-4959
| Abstract »
| Full Text »
| PDF »
|
|
