This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Florin, L. Articles by Sapp, M. Search for Related Content PubMed PubMed Citation Articles by Florin, L. Articles by Sapp, M.

Nuclear Translocation of Papillomavirus Minor Capsid Protein L2 Requires Hsc70

Institute for Medical Microbiology and Hygiene, Johannes Gutenberg-Universität, D-55101 Mainz,¹ Heinrich Pette Institute for Experimental Virology and Immunology, Universität Hamburg, D-20206 Hamburg,² German Cancer Research Institute, ATV, D-69120 Heidelberg, Germany³

Received 18 December 2003/ Accepted 11 February 2004

Minor capsid protein L2 of papillomaviruses plays an essential role in virus assembly by recruiting viral components to PML bodies, the proposed sites of virus morphogenesis. We demonstrate here that the function of L2 in virus assembly requires the chaperone Hsc70. Hsc70 was found dispersed in naturally infected keratinocytes and cultured cells. A dramatic relocation of Hsc70 from the cytoplasm to PML bodies was induced in these cells by L2 expression. Hsc70-L2 complex formation was confirmed by coimmunoprecipitation. The complex was modulated by the cochaperones Hip and Bag-1, which stabilize and destabilize Hsc70-substrate complexes, respectively. Cytoplasmic depletion of Hsc70 caused retention of wild-type and N-terminally truncated L2, but not of C-terminally truncated L2, in the cytoplasm. This retention was partially reversed by overexpression of Hsc70 fused to green fluorescent protein but not by ATPase-negative Hsc70. Hsc70 associated with L1-L2 virus-like particles (VLPs) but not with VLPs composed either of L1 alone or of L1 and C-terminally truncated L2. Moreover, displacement of Hsc70 from L1-L2 VLPs by encapsidation of DNA, generating pseudovirions, was found. These data indicate that Hsc70 transiently associates with viral capsids during the integration of L2, possibly via the L2 C terminus. Completion of virus assembly results in displacement of Hsc70 from virions.

This article has been cited by other articles:

• Salas-Benito, J., Valle, J. R.-D., Salas-Benito, M., Ceballos-Olvera, I., Mosso, C., del Angel, R. M. (2007). Evidence that the 45-kD Glycoprotein, Part of a Putative Dengue Virus Receptor Complex in the Mosquito Cell Line C6/36, Is a Heat-Shock Related Protein. Am J Trop Med Hyg 77: 283-290 [Abstract] [Full Text]  
• Florin, L., Becker, K. A., Lambert, C., Nowak, T., Sapp, C., Strand, D., Streeck, R. E., Sapp, M. (2006). Identification of a Dynein interacting domain in the papillomavirus minor capsid protein l2.. J. Virol. 80: 6691-6696 [Abstract] [Full Text]  
• Kamper, N., Day, P. M., Nowak, T., Selinka, H.-C., Florin, L., Bolscher, J., Hilbig, L., Schiller, J. T., Sapp, M. (2006). A Membrane-Destabilizing Peptide in Capsid Protein L2 Is Required for Egress of Papillomavirus Genomes from Endosomes. J. Virol. 80: 759-768 [Abstract] [Full Text]  
• Bechtel, J. T., Winant, R. C., Ganem, D. (2005). Host and Viral Proteins in the Virion of Kaposi's Sarcoma-Associated Herpesvirus. J. Virol. 79: 4952-4964 [Abstract] [Full Text]  
• Darshan, M. S., Lucchi, J., Harding, E., Moroianu, J. (2004). The L2 Minor Capsid Protein of Human Papillomavirus Type 16 Interacts with a Network of Nuclear Import Receptors. J. Virol. 78: 12179-12188 [Abstract] [Full Text]