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Journal of Virology, June 2007, p. 5841-5849, Vol. 81, No. 11
0022-538X/07/$08.00+0     doi:10.1128/JVI.00096-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Infectivity Determinants of the Hepatitis B Virus Pre-S Domain Are Confined to the N-Terminal 75 Amino Acid Residues{triangledown}

Matthieu Blanchet1 and Camille Sureau1,2*

Laboratoire de Virologie Moléculaire, INTS, Paris, France,1 Department of Virology and Immunology, Southwest Foundation for Biomedical Research, San Antonio, Texas 782282

Received 15 January 2007/ Accepted 9 March 2007

The N-terminal pre-S domain of the large hepatitis B virus (HBV) envelope protein plays a pivotal role at the initial step of the viral entry pathway. In the present study, the entire pre-S domain was mapped for infectivity determinants, following a reverse-genetics approach and using in vitro infection assays with hepatitis delta virus (HDV) or HBV particles. The results demonstrate that lesions created within the N-terminal 75 amino acids of the pre-S region abrogate infectivity, whereas mutations between amino acids 76 and 113, overlapping the matrix domain, had no effect. In contrast to the results of a recent study (L. Stoeckl, A. Funk, A. Kopitzki, B. Brandenburg, S. Oess, H. Will, H. Sirma, and E. Hildt, Proc. Natl. Acad. Sci. 103:6730-6734, 2006), the deletion of a cell membrane translocation motif (TLM) located between amino acids 148 and 161 at the C terminus of pre-S2 did not interfere with the infectivity of the resulting HDV or HBV mutants. Furthermore, a series of large deletions overlapping the pre-S2 domain were compatible with infectivity, although the efficiency of infection was reduced when the deletions extended to the pre-S1 domain. Overall, the results demonstrate that the activity of the pre-S domain at viral entry solely depends on the integrity of its first 75 amino acids and thus excludes any function of the matrix domain or TLM.

* Corresponding author. Mailing address: Laboratoire de Virologie Moléculaire, Institut National de la Transfusion Sanguine, 6 Rue Alexandre-Cabanel, 75739 Paris, France. Phone: (33) 1 44 49 30 56. Fax: (33) 1 44 49 30 59. E-mail: csureau{at}ints.fr

{triangledown} Published ahead of print on 21 March 2007.

Journal of Virology, June 2007, p. 5841-5849, Vol. 81, No. 11
0022-538X/07/$08.00+0     doi:10.1128/JVI.00096-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Le Duff, Y., Blanchet, M., Sureau, C. (2009). The Pre-S1 and Antigenic Loop Infectivity Determinants of the Hepatitis B Virus Envelope Proteins Are Functionally Independent. J. Virol. 83: 12443-12451 [Abstract] [Full Text]  
  • 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]  
  • Salisse, J., Sureau, C. (2009). A Function Essential to Viral Entry Underlies the Hepatitis B Virus "a" Determinant. J. Virol. 83: 9321-9328 [Abstract] [Full Text]  
  • Abou-Jaoude, G., Sureau, C. (2007). Entry of Hepatitis Delta Virus Requires the Conserved Cysteine Residues of the Hepatitis B Virus Envelope Protein Antigenic Loop and Is Blocked by Inhibitors of Thiol-Disulfide Exchange. J. Virol. 81: 13057-13066 [Abstract] [Full Text]  
  • Lepere, C., Regeard, M., Le Seyec, J., Gripon, P. (2007). The Translocation Motif of Hepatitis B Virus Envelope Proteins Is Dispensable for Infectivity. J. Virol. 81: 7816-7818 [Abstract] [Full Text]  


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