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Journal of Virology, August 2004, p. 8078-8084, Vol. 78, No. 15
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.15.8078-8084.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Isolation of Capsid Protein Dimers from the Tick-Borne Encephalitis Flavivirus and In Vitro Assembly of Capsid-Like Particles

Stefan Kiermayr,1 Regina M. Kofler,1 Christian W. Mandl,1 Paul Messner,2 and Franz X. Heinz1*

Institute of Virology, Medical University of Vienna,1 Center for Ultrastructure Research, University of Natural Resources and Applied Life Sciences, Vienna, Austria2

Received 26 November 2003/ Accepted 15 March 2004

Flaviviruses have a spherical capsid that is composed of multiple copies of a single capsid protein and, in contrast to the viral envelope, apparently does not have an icosahedral structure. So far, attempts to isolate distinct particulate capsids and soluble forms of the capsid protein from purified virions as well as to assemble capsid-like particles in vitro have been largely unsuccessful. Here we describe the isolation of nucleocapsids from tick-borne encephalitis (TBE) virus and their disintegration into a capsid protein dimer by high-salt treatment. Purified capsid protein dimers could be assembled in vitro into capsid-like particles when combined with in vitro transcribed viral RNA. Particulate structures could also be obtained when single-stranded DNA oligonucleotides were used. These data suggest that the dimeric capsid protein functions as a basic building block in the assembly process of flaviviruses.

* Corresponding author. Mailing address: Institute of Virology, Medical University of Vienna, Kinderspitalgasse 15, A-1095 Vienna, Austria. Phone: 43 1 4277, ext. 79510. Fax: 43 1 4277 9795. E-mail: franz.x.heinz{at}meduniwien.ac.at.

Journal of Virology, August 2004, p. 8078-8084, Vol. 78, No. 15
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.15.8078-8084.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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