This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Mir, M. A.
Right arrow Articles by Panganiban, A. T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mir, M. A.
Right arrow Articles by Panganiban, A. T.

 Previous Article  |  Next Article 

Journal of Virology, February 2005, p. 1824-1835, Vol. 79, No. 3
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.3.1824-1835.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Hantavirus Nucleocapsid Protein Recognizes Specific Features of the Viral RNA Panhandle and Is Altered in Conformation upon RNA Binding

M. A. Mir and A. T. Panganiban*

Department of Molecular Genetics and Microbiology, University of New Mexico Health Sciences Center, Albuquerque, New Mexico

Received 27 May 2004/ Accepted 21 September 2004

Hantaviruses are tripartite negative-sense RNA viruses and members of the Bunyaviridae family. The nucleocapsid (N) protein is the principal structural component of the viral capsid. N forms a stable trimer that specifically recognizes the panhandle structure formed by the viral RNA termini. We used trimeric glutathione S-transferase (GST)-N protein and small RNA panhandles to examine the requirements for specific recognition by Sin Nombre hantavirus N. Trimeric GST-N recognizes the panhandles of the three viral RNAs (S, M, and L) with high affinity, whereas the corresponding plus-strand panhandles of the complementary RNA are recognized with lower affinity. Based on analysis of nucleotide substitutions that alter either the higher-order structure of the panhandle or the primary sequence of the panhandle, both secondary structure and primary sequence are necessary for stable interaction with N. A panhandle 23 nucleotides long is necessary and sufficient for high-affinity binding by N, and stoichiometry calculations indicate that a single N trimer interacts with a single panhandle. Surprisingly, displacement of the panhandle structure away from the terminus does not eliminate recognition by N. The binding of N to the panhandle is an entropy-driven process resulting in initial stable N-RNA interaction followed by a conformational change in N. Taken together, these data provide insight into the molecular events that take place during interaction of N with the panhandle and suggest that specific high-affinity interaction between an RNA binding domain of trimeric N and the panhandle is required for encapsidation of the three viral RNAs.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of New Mexico Health Sciences Center, Albuquerque, NM 87131. Phone: (505) 272-4214. Fax: (505) 272-9912. E-mail: apanganiban{at}salud.unm.edu.

Journal of Virology, February 2005, p. 1824-1835, Vol. 79, No. 3
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.3.1824-1835.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Mohl, B.-P., Barr, J. N. (2009). Investigating the specificity and stoichiometry of RNA binding by the nucleocapsid protein of Bunyamwera virus. RNA 15: 391-399 [Abstract] [Full Text]  
  • Wang, Y., Boudreaux, D. M., Estrada, D. F., Egan, C. W., St. Jeor, S. C., De Guzman, R. N. (2008). NMR Structure of the N-terminal Coiled Coil Domain of the Andes Hantavirus Nucleocapsid Protein. J. Biol. Chem. 283: 28297-28304 [Abstract] [Full Text]  
  • Ogg, M. M., Patterson, J. L. (2007). RNA Binding Domain of Jamestown Canyon Virus S Segment RNAs. J. Virol. 81: 13754-13760 [Abstract] [Full Text]  
  • Ramanathan, H. N., Chung, D.-H., Plane, S. J., Sztul, E., Chu, Y.-k., Guttieri, M. C., McDowell, M., Ali, G., Jonsson, C. B. (2007). Dynein-Dependent Transport of the Hantaan Virus Nucleocapsid Protein to the Endoplasmic Reticulum-Golgi Intermediate Compartment. J. Virol. 81: 8634-8647 [Abstract] [Full Text]  
  • Mir, M. A., Brown, B., Hjelle, B., Duran, W. A., Panganiban, A. T. (2006). Hantavirus N Protein Exhibits Genus-Specific Recognition of the Viral RNA Panhandle. J. Virol. 80: 11283-11292 [Abstract] [Full Text]  
  • Mir, M. A., Panganiban, A. T. (2006). Characterization of the RNA chaperone activity of hantavirus nucleocapsid protein.. J. Virol. 80: 6276-6285 [Abstract] [Full Text]  
  • MIR, M. A., PANGANIBAN, A. T. (2006). The bunyavirus nucleocapsid protein is an RNA chaperone: Possible roles in viral RNA panhandle formation and genome replication. RNA 12: 272-282 [Abstract] [Full Text]  
  • Ivanyi-Nagy, R., Kanevsky, I., Gabus, C., Lavergne, J.-P., Ficheux, D., Penin, F., Fosse, P., Darlix, J.-L. (2006). Analysis of hepatitis C virus RNA dimerization and core-RNA interactions.. Nucleic Acids Res 34: 2618-2633 [Abstract] [Full Text]  
  • Le May, N., Gauliard, N., Billecocq, A., Bouloy, M. (2005). The N Terminus of Rift Valley Fever Virus Nucleoprotein Is Essential for Dimerization. J. Virol. 79: 11974-11980 [Abstract] [Full Text]  
  • Severson, W., Xu, X., Kuhn, M., Senutovitch, N., Thokala, M., Ferron, F., Longhi, S., Canard, B., Jonsson, C. B. (2005). Essential Amino Acids of the Hantaan Virus N Protein in Its Interaction with RNA. J. Virol. 79: 10032-10039 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»