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Journal of Virology, July 2007, p. 7816-7818, Vol. 81, No. 14
0022-538X/07/$08.00+0     doi:10.1128/JVI.00224-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The Translocation Motif of Hepatitis B Virus Envelope Proteins Is Dispensable for Infectivity{triangledown}

Charlotte Lepère, Morgane Régeard, Jacques Le Seyec, and Philippe Gripon*

INSERM U522, IFR 140, Hôpital de Pontchaillou, Avenue Henri Le Guilloux, Rennes F-35033, France, and Université de Rennes 1, Rennes F-35000, France

Received 1 February 2007/ Accepted 2 May 2007

The early events of hepatitis B virus (HBV) infection remain unclear. In 2006, Stoeckl et al. proposed a new entry mechanism involving a translocation motif (TLM) present in the pre-S2 domain of envelope proteins (L. Stoeckl, A. Funk, A. Kopitzki, B. Brandenburg, S. Oess, H. Will, H. Sirma, and E. Hildt, Proc. Natl. Acad. Sci. USA 103:6730-6734, 2006). After receptor binding and internalization into the endosomal compartment, this motif would allow the translocation of HBV particles through the endosomal membrane into the cytosol. In this study we have used two different mutated viruses containing a truncated TLM and showed their ability to infect human hepatocytes in primary culture, thus demonstrating the dispensability of the TLM for HBV infectivity.


* Corresponding author. Mailing address: INSERM U522, Hôpital de Pontchaillou, Avenue Henri le Guilloux, Rennes Cedex 35033, France. Phone: (33) 2-99-54-74-08. Fax: (33) 2-99-54-01-37. E-mail: philippe.gripon{at}univ-rennes1.fr

{triangledown} Published ahead of print on 9 May 2007.


Journal of Virology, July 2007, p. 7816-7818, Vol. 81, No. 14
0022-538X/07/$08.00+0     doi:10.1128/JVI.00224-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Lepere-Douard, C., Trotard, M., Le Seyec, J., Gripon, P. (2009). The First Transmembrane Domain of the Hepatitis B Virus Large Envelope Protein Is Crucial for Infectivity. J. Virol. 83: 11819-11829 [Abstract] [Full Text]