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Journal of Virology, September 2006, p. 9073-9081, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.00515-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Oligomerization of Hantavirus Nucleocapsid Protein: Analysis of the N-Terminal Coiled-Coil Domain

Agne Alminaite,1 Vera Halttunen,1,2 Vibhor Kumar,3 Antti Vaheri,1 Liisa Holm,2,4 and Alexander Plyusnin1*

Department of Virology, Haartman Institute, P.O. Box 21, FIN-00014 University of Helsinki, Helsinki, Finland,1 Institute of Biotechnology,2 Department of Biosciences, P.O. Box 56, FIN-00014 University of Helsinki, Helsinki, Finland,4 Laboratory of Computational Engineering, P.O. Box 9203, FIN-02015 Helsinki University of Technology, Helsinki, Finland3

Received 13 March 2006/ Accepted 23 June 2006

Hantaviruses constitute a genus in the family Bunyaviridae. They are enveloped negative-strand RNA viruses with a tripartite genome encoding the nucleocapsid (N) protein, the two surface glycoproteins Gn and Gc, and an RNA-dependent RNA polymerase. The N protein is the most abundant component of the virion; it encapsidates genomic RNA segments forming ribonucleoproteins and participates in genome transcription and replication as well as virus assembly. In the course of RNA encapsidation, N protein forms intermediate trimers via head-to-head and tail-to-tail interactions. We analyzed the amino-terminal trimerization domain (amino acid residues 1 to 77) of Tula hantavirus using computer modeling, mammalian two-hybrid assay, and immunofluorescence assay. The results obtained were consistent with the existence of an antiparallel coiled-coil stabilized by interactions between hydrophobic residues. Residues L44, V51, and L58 were important for the N-N interaction; other residues, e.g., L25 and V32, also made a contribution, albeit a modest one. Our alignments of the N-terminal domain of the hantaviral N proteins suggest the coiled-coil structure, and hence the mode of N-protein oligomerization, is conserved among hantaviruses.

* Corresponding author. Mailing address: Department of Virology, Haartman Institute, P.O. Box 21, FIN-00014 University of Helsinki, Helsinki, Finland. Phone: 358-9-19126486. Fax: 358-9-19126491. E-mail: alexander.plyusnin{at}helsinki.fi.

Journal of Virology, September 2006, p. 9073-9081, Vol. 80, No. 18
0022-538X/06/$08.00+0     doi:10.1128/JVI.00515-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • 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]  
  • Alminaite, A., Backstrom, V., Vaheri, A., Plyusnin, A. (2008). Oligomerization of hantaviral nucleocapsid protein: charged residues in the N-terminal coiled-coil domain contribute to intermolecular interactions. J. Gen. Virol. 89: 2167-2174 [Abstract] [Full Text]  


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