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Journal of Virology, February 2001, p. 1968-1977, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1968-1977.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Signals for Bidirectional Nucleocytoplasmic Transport in the Duck Hepatitis B Virus Capsid Protein

Helene Mabit,dagger Klaus M. Breiner,Dagger Andreas Knaust, Beate Zachmann-Brand, and Heinz Schaller*

Mikrobiologie and Zentrum für Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany

Received 31 August 2000/Accepted 16 November 2000

Hepadnavirus genome replication involves cytoplasmic and nuclear stages, requiring balanced targeting of cytoplasmic nucleocapsids to the nuclear compartment. In this study, we analyze the signals determining capsid compartmentalization in the duck hepatitis B virus (DHBV) animal model, as this system also allows us to study hepadnavirus infection of cultured primary hepatocytes. Using fusions to the green fluorescent protein as a functional assay, we have identified a nuclear localization signal (NLS) that mediates nuclear pore association of the DHBV nucleocapsid and nuclear import of DHBV core protein (DHBc)-derived polypeptides. The DHBc NLS mapped is unique. It bears homology to repetitive NLS elements previously identified near the carboxy terminus of the capsid protein of hepatitis B virus, the human prototype of the hepadnavirus family, but it maps to a more internal position. In further contrast to the hepatitis B virus core protein NLS, the DHBc NLS is not positioned near phosphorylation target sites that are generally assumed to modulate nucleocytoplasmic transport. In functional assays with a knockout mutant, the DHBc NLS was found to be essential for nuclear pore association of the nucleocapsid. The NLS was found to be also essential for virus production from the full-length DHBV genome in transfected cells and from hepatocytes infected with transcomplemented mutant virus. Finally, the DHBc additionally displayed activity indicative of a nuclear export signal, presumably counterbalancing NLS function in the productive state of the infected cell and thereby preventing nucleoplasmic accumulation of nucleocapsids.

* Corresponding author. Mailing address: ZMBH, University of Heidelberg, Im Neuenheimer Feld 282, 69120 Heidelberg, Germany. Phone: 49 6221 546885. Fax: 49 6221 545893. E-mail: hshd{at}zmbh.uni-heidelberg.de.

dagger Present address: Institute of Zoology, 8057 Zürich, Switzerland.

Dagger Present address: Department of Biochemistry, Swiss Institute of Technology, 8092 Zürich, Switzerland.

Journal of Virology, February 2001, p. 1968-1977, Vol. 75, No. 4
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.4.1968-1977.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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