Interaction between molecules of hantavirus nucleocapsid protein

Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland 1 Author for correspondence: Pasi Kaukinen. Fax +358 9 19126491. e-mail Pasi.Kaukinen{at}helsinki.fi Intermolecular interactions of Tula hantavirus N (nucleocapsid) protein were detected in the yeast two...

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Bibliographic Details
Published in:Journal of general virology 2001-08, Vol.82 (8), p.1845-1853
Main Authors: Kaukinen, Pasi, Koistinen, Vesa, Vapalahti, Olli, Vaheri, Antti, Plyusnin, Alexander
Format: Article
Language:English
Subjects:
AN protein
Animals
Baculoviridae - genetics
Barium - pharmacology
Calcium - pharmacology
Capsid - metabolism
Capsid Proteins
Cations, Divalent
Dimerization
Dose-Response Relationship, Drug
Enzyme-Linked Immunosorbent Assay
Hantavirus
Hantavirus - metabolism
Magnesium - pharmacology
Manganese - pharmacology
Nucleocapsid Proteins - genetics
Nucleocapsid Proteins - metabolism
Protein Binding
Protein Folding
Recombinant Proteins - metabolism
Two-Hybrid System Techniques
Viral Core Proteins - metabolism
Virus Assembly
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Summary:Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland 1 Author for correspondence: Pasi Kaukinen. Fax +358 9 19126491. e-mail Pasi.Kaukinen{at}helsinki.fi Intermolecular interactions of Tula hantavirus N (nucleocapsid) protein were detected in the yeast two-hybrid system, prompting further attempts to study this phenomenon. Using chemical cross-linking and immunoblotting it was shown that the N protein from purified virus and from infected cell lysates as well as recombinant protein produced in a baculovirus expression system are capable of forming dimers, trimers and multimers, thus confirming the capacity of the protein molecules to interact with each other. An ELISA format was developed in which molecules of the recombinant N protein were shown to associate non-covalently, via electrostatic interactions. Divalent cations (Ca 2+ , Mn 2+ , Mg 2+ , Ba 2+ ) enhanced the process 3- to 8-fold suggesting that adequate folding of the N protein is crucial for the association. Based on these data a model for hantavirus nucleocapsid assembly is proposed, in which N molecules first trimerize around the viral RNA molecule, and then the trimers gradually assemble forming longer multimers.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-82-8-1845