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Journal of Virology, December 2004, p. 13669-13677, Vol. 78, No. 24
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.24.13669-13677.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Oligomerization of Hantavirus N Protein: C-Terminal {alpha}-Helices Interact To Form a Shared Hydrophobic Space

Pasi Kaukinen,1,{dagger} Vibhor Kumar,2,{dagger} Kirsi Tulimäki,1 Peter Engelhardt,1,2 Antti Vaheri,1* and Alexander Plyusnin1

Department of Virology, Haartman Institute, University of Helsinki,1 Laboratory of Computational Engineering, Helsinki University of Technology, Helsinki, Finland2

Received 4 May 2004/ Accepted 3 August 2004

The structure of the nucleocapsid protein of bunyaviruses has not been defined. Earlier we have shown that Tula hantavirus N protein oligomerization is dependent on the C-terminal domains. Of them, the helix-loop-helix motif was found to be an essential structure. Computer modeling predicted that oligomerization occurs via helix protrusions, and the shared hydrophobic space formed by amino acids residues 380-IILLF-384 in the first helix and 413-LI-414 in the second helix is responsible for stabilizing the interaction. The model was validated by two approaches. First, analysis of the oligomerization capacity of the N protein mutants performed with the mammalian two-hybrid system showed that both preservation of the helix structure and formation of the shared hydrophobic space are crucial for the interaction. Second, oligomerization was shown to be a prerequisite for the granular pattern of transiently expressed N protein in transfected cells. N protein trimerization was supported by three-dimensional reconstruction of the N protein by electron microscopy after negative staining. Finally, we discuss how N protein trimerization could occur.

* Corresponding author: Mailing address: Department of Virology, Haartman Institute, P.O. Box 21, FI-00014 University of Helsinki, Finland. Phone: 358 9 19126490. Fax: 358 9 19126491. E-mail: antti.vaheri{at}helsinki.fi.

{dagger} These authors contributed equally to the paper.

Journal of Virology, December 2004, p. 13669-13677, Vol. 78, No. 24
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.24.13669-13677.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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