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
Services
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 Blanchet, M.
Right arrow Articles by Sureau, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Blanchet, M.
Right arrow Articles by Sureau, C.

 Previous Article  |  Next Article 

Journal of Virology, December 2006, p. 11935-11945, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.00621-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Analysis of the Cytosolic Domains of the Hepatitis B Virus Envelope Proteins for Their Function in Viral Particle Assembly and Infectivity{triangledown}

Matthieu Blanchet1 and Camille Sureau1,2*

Laboratoire de Virologie, INTS, Paris, France 75739,1 Department of Virology and Immunology, Southwest Foundation for Biomedical Research, San Antonio, Texas 782282

Received 28 March 2006/ Accepted 26 September 2006

The hepatitis B virus (HBV) envelope proteins have the ability to assemble three types of viral particles, (i) the empty subviral particles (SVPs), (ii) the mature HBV virions, and (iii) the hepatitis delta virus (HDV) particles, in cells that are coinfected with HBV and HDV. To gain insight into the function of the HBV envelope proteins in morphogenesis of HBV or HDV virions, we have investigated subdomains of the envelope proteins that have been shown or predicted to lie at the cytosolic face of the endoplasmic reticulum membrane during synthesis, a position prone to interaction with the inner core structure. These domains, referred to here as cytosolic loops I and II (CYL-I and -II, respectively), were subjected to mutagenesis. The mutations were introduced in the three HBV envelope proteins, designated small, middle, and large (S-HBsAg, M-HBsAg, and L-HBsAg, respectively). The mutants were expressed in HuH-7 cells to evaluate their capacity for self-assembly and formation of HBV or HDV virions when HBV nucleocapsid or HDV ribonucleoprotein, respectively, was provided. We found that SVP-competent CYL-I mutations between positions 23 and 78 of the S domain were permissive to HBV or HDV virion assembly. One mutation (P29A) was permissive for synthesis of the S- and M-HBsAg but adversely affected the synthesis or stability of L-HBsAg, thereby preventing the assembly of HBV virions. Furthermore, using an in vitro infection assay based on the HepaRG cells and the HDV model, we have shown that particles coated with envelope proteins bearing CYL-I mutations were fully infectious, hence indicating the absence of an infectivity determinant in this region. Finally, we demonstrated that the tryptophan residues at positions 196, 199, and 201 in CYL-II, which were shown to exert a matrix function for assembly of HDV particles (I. Komla-Soukha and C. Sureau, J. Virol. 80:4648-4655, 2006), were dispensable for both assembly and infectivity of HBV virions.

* Corresponding author. Mailing address: Laboratoire de Virologie, Institut National de la Transfusion Sanguine, 6 rue Alexandre Cabanel, 75739 Paris, France. E-mail: csureau{at}ints.fr.

{triangledown} Published ahead of print on 4 October 2006.

Journal of Virology, December 2006, p. 11935-11945, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.00621-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Huang, C., Chang, S. C., Yang, H.-C., Chien, C.-L., Chang, M.-F. (2009). Clathrin-Mediated Post-Golgi Membrane Trafficking in the Morphogenesis of Hepatitis Delta Virus. J. Virol. 83: 12314-12324 [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]  
  • Garcia, T., Li, J., Sureau, C., Ito, K., Qin, Y., Wands, J., Tong, S. (2009). Drastic Reduction in the Production of Subviral Particles Does Not Impair Hepatitis B Virus Virion Secretion. J. Virol. 83: 11152-11165 [Abstract] [Full Text]  
  • Hantz, O., Parent, R., Durantel, D., Gripon, P., Guguen-Guillouzo, C., Zoulim, F. (2009). Persistence of the hepatitis B virus covalently closed circular DNA in HepaRG human hepatocyte-like cells. J. Gen. Virol. 90: 127-135 [Abstract] [Full Text]  
  • Shih, H. H., Jeng, K.-S., Syu, W.-J., Huang, Y.-H., Su, C.-W., Peng, W.-L., Sheen, I-J., Wu, J.-C. (2008). Hepatitis B Surface Antigen Levels and Sequences of Natural Hepatitis B Virus Variants Influence the Assembly and Secretion of Hepatitis D Virus. J. Virol. 82: 2250-2264 [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]  
  • Blanchet, M., Sureau, C. (2007). Infectivity Determinants of the Hepatitis B Virus Pre-S Domain Are Confined to the N-Terminal 75 Amino Acid Residues. J. Virol. 81: 5841-5849 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»