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Journal of Virology, February 2004, p. 1121-1128, Vol. 78, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.3.1121-1128.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Nuclear Localization but Not PML Protein Is Required for Incorporation of the Papillomavirus Minor Capsid Protein L2 into Virus-Like Particles

Katrin A. Becker,1 Luise Florin,1 Cornelia Sapp,1 Gerd G. Maul,2 and Martin Sapp1*

Institute of Medical Microbiology and Hygiene, University of Mainz, 55101 Mainz, Germany,1 The Wistar Institute, Philadelphia, Pennsylvania 191042

Received 1 September 2003/ Accepted 21 October 2003

Recent reports suggest that nuclear domain(s) 10 (ND10) is the site of papillomavirus morphogenesis. The viral genome replicates in or close to ND10. In addition, the minor capsid protein, L2, accumulates in these subnuclear structures and recruits the major capsid protein, L1. We have now used cell lines deficient for promyelocytic leukemia (PML) protein, the main structural component of ND10, to study the role of this nuclear protein for L2 incorporation into virus-like particles (VLPs). L2 expressed in PML protein knockout (PML-/-) cells accumulated in nuclear dots, which resemble L2 aggregates forming at ND10 in PML protein-containing cells. These L2 assemblies also attracted L1 and the transcriptional repressor Daxx, suggesting that they are functional in the absence of PML protein. In addition, L2-containing VLPs assembled in PML-/- cells. In order to analyze whether incorporation of L2 into VLPs requires any specific subcellular localization, an L1 mutant defective for nuclear transport and L2 mutants deficient in nuclear translocation and/or ND10 localization were constructed. Using this approach, we identified two independent L2 domains interacting with L1. Mutant L2 proteins not accumulating in ND10 were incorporated into VLPs. Mutant L1 protein, which assembled into VLPs in the cytoplasm, did not incorporate L2 defective for nuclear translocation. The same mutant L2 protein, which passively diffuses into the nucleus, is incorporated into wild-type L1-VLPs in the nucleus. Our data demonstrate that the incorporation of L2 into VLPs requires nuclear but not ND10 localization.

* Corresponding author. Mailing address: Institute of Medical Microbiology and Hygiene, University of Mainz, Hochhaus am Augustusplatz, 55101 Mainz, Germany. Phone: 49-6131-393-0211. Fax: 49-6131-393-2359. E-mail: sapp{at}mail.uni-mainz.de.

Journal of Virology, February 2004, p. 1121-1128, Vol. 78, No. 3
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.3.1121-1128.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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