This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Patterson, N. A.
Right arrow Articles by Ozbun, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Patterson, N. A.
Right arrow Articles by Ozbun, M. A.

 Previous Article  |  Next Article 

Journal of Virology, June 2005, p. 6838-6847, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6838-6847.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Human Papillomavirus Type 31b Infection of Human Keratinocytes Does Not Require Heparan Sulfate

Nicole A. Patterson, Jessica L. Smith, and Michelle A. Ozbun*

Department of Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, New Mexico

Received 30 September 2004/ Accepted 18 January 2005

Oncogenic human papillomaviruses (HPVs) are difficult to study experimentally as they replicate at low levels in vivo. This has precluded the purification of high-risk HPV virions from in vivo lesions. Virus-like particles (VLPs) and pseudovirions from low- and high-risk HPV types can emulate various aspects of HPV virion attachment and infections. These studies suggest that HPV infection is mediated by {alpha}6-integrin and/or heparan-sulfonated receptors. However, whether VLPs and pseudovirions accurately reflect the infection process of HPV virions has not been verified. We generated infectious HPV31b virions from organotypic (raft) tissues and performed experimental infections in a variety of cells. Successful infection following viral attachment, internalization, and nuclear transport was assayed by detecting newly synthesized, spliced HPV transcripts using reverse transcription (RT)-PCR or RT-quantitative PCR. Most human epithelial cells were infected with HPV31b at a multiplicity of infection as low as 1 to 10 viral genome equivalents per cell. HPV31b infection was detected in other cell lines, including COS-7 monkey kidney cells, but higher viral multiplicities of infection were required. Heparin preparations of various molecular weights or heparinase I treatment of cells prevented HPV31b infection of COS-7 cells and C-33A human cervical cancer cells in reproducible and dose-dependent manners. However, these reagents were unable to block infection of human keratinocytes, including HaCaT and N/TERT-1 cells and low-passage human foreskin keratinocytes. These data suggest that HPV31b infection of human keratinocytes, the natural host cell for HPV infections in vivo, does not require a heparan-sulfonated receptor, whereas heparan sulfate is important for infection of some other cells.

* Corresponding author. Mailing address: Department of Molecular Genetics and Microbiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131. Phone: 505-272-4950. Fax: 505-272-9912. E-mail: mozbun{at}salud.unm.edu.

Journal of Virology, June 2005, p. 6838-6847, Vol. 79, No. 11
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.11.6838-6847.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Broutian, T. R., Brendle, S. A., Christensen, N. D. (2010). Differential binding patterns to host cells associated with particles of several human alphapapillomavirus types. J. Gen. Virol. 91: 531-540 [Abstract] [Full Text]  
  • Lace, M. J., Anson, J. R., Klingelhutz, A. J., Lee, J. H., Bossler, A. D., Haugen, T. H., Turek, L. P. (2009). Human Papillomavirus (HPV) Type 18 Induces Extended Growth in Primary Human Cervical, Tonsillar, or Foreskin Keratinocytes More Effectively than Other High-Risk Mucosal HPVs. J. Virol. 83: 11784-11794 [Abstract] [Full Text]  
  • Conway, M.J., Meyers, C. (2009). Replication and Assembly of Human Papillomaviruses. JDR 88: 307-317 [Abstract] [Full Text]  
  • Johnson, K. M., Kines, R. C., Roberts, J. N., Lowy, D. R., Schiller, J. T., Day, P. M. (2009). Role of Heparan Sulfate in Attachment to and Infection of the Murine Female Genital Tract by Human Papillomavirus. J. Virol. 83: 2067-2074 [Abstract] [Full Text]  
  • Smith, J. L., Campos, S. K., Wandinger-Ness, A., Ozbun, M. A. (2008). Caveolin-1-Dependent Infectious Entry of Human Papillomavirus Type 31 in Human Keratinocytes Proceeds to the Endosomal Pathway for pH-Dependent Uncoating. J. Virol. 82: 9505-9512 [Abstract] [Full Text]  
  • Selinka, H.-C., Florin, L., Patel, H. D., Freitag, K., Schmidtke, M., Makarov, V. A., Sapp, M. (2007). Inhibition of Transfer to Secondary Receptors by Heparan Sulfate-Binding Drug or Antibody Induces Noninfectious Uptake of Human Papillomavirus. J. Virol. 81: 10970-10980 [Abstract] [Full Text]  
  • Smith, J. L., Campos, S. K., Ozbun, M. A. (2007). Human Papillomavirus Type 31 Uses a Caveolin 1- and Dynamin 2-Mediated Entry Pathway for Infection of Human Keratinocytes. J. Virol. 81: 9922-9931 [Abstract] [Full Text]  
  • Culp, T. D., Budgeon, L. R., Marinkovich, M. P., Meneguzzi, G., Christensen, N. D. (2006). Keratinocyte-Secreted Laminin 5 Can Function as a Transient Receptor for Human Papillomaviruses by Binding Virions and Transferring Them to Adjacent Cells. J. Virol. 80: 8940-8950 [Abstract] [Full Text]  
  • Pyeon, D., Lambert, P. F., Ahlquist, P. (2005). Production of infectious human papillomavirus independently of viral replication and epithelial cell differentiation. Proc. Natl. Acad. Sci. USA 102: 9311-9316 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»