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 Grgacic, E. V. L.
Right arrow Articles by Schaller, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Grgacic, E. V. L.
Right arrow Articles by Schaller, H.

 Previous Article  |  Next Article 

Journal of Virology, March 2000, p. 2455-2458, Vol. 74, No. 5
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Hepadnavirus Envelope Topology: Insertion of a Loop Region in the Membrane and Role of S in L Protein Translocation

E. V. L. Grgacic,1,* C. Kuhn,2 and H. Schaller2

Macfarlane Burnet Centre for Medical Research, Fairfield, Victoria, Australia,1 and Zentrum für Molekulare Biologie, Universität Heidelberg, 69120 Heidelberg, Germany2

Received 7 September 1999/Accepted 30 November 1999

A unique feature of the large hepadnavirus envelope protein (L) is its mixed transmembrane topology, resulting from partial posttranslational translocation of the pre-S domain. Using protease protection analysis, we demonstrate for duck hepatitis B virus an essential role for the small envelope protein (S) in this process, providing the first experimental evidence for an S translocation channel. Further analysis revealed that the presumed cytoplasmic loop between TM1 and TM2 in the C-terminal S domain is membrane embedded and protrudes to the particle surface. These data suggest that some L molecules form a highly folded, potentially spring-loaded topology with five membrane-spanning regions and a membrane-traversing pre-S chain.

* Corresponding author. Mailing address: Macfarlane Burnet Centre for Medical Research, Yarra Bend Rd., P.O. Box 254, Fairfield, Victoria 3078, Australia. Phone: 61 3 9282 2109. Fax: 61 3 9282 2100. E-mail: grgacic{at}burnet.edu.au.

Journal of Virology, March 2000, p. 2455-2458, Vol. 74, No. 5
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Chojnacki, J., Anderson, D. A., Grgacic, E. V. L. (2005). A Hydrophobic Domain in the Large Envelope Protein Is Essential for Fusion of Duck Hepatitis B Virus at the Late Endosome. J. Virol. 79: 14945-14955 [Abstract] [Full Text]  
  • Grgacic, E. V. L., Anderson, D. A. (2005). St, a Truncated Envelope Protein Derived from the S Protein of Duck Hepatitis B Virus, Acts as a Chaperone for the Folding of the Large Envelope Protein. J. Virol. 79: 5346-5352 [Abstract] [Full Text]  
  • Grgacic, E. V. L. (2002). Identification of structural determinants of the first transmembrane domain of the small envelope protein of duck hepatitis B virus essential for particle morphogenesis. J. Gen. Virol. 83: 1635-1644 [Abstract] [Full Text]  
  • Clayton, R. F., Owsianka, A., Patel, A. H. (2001). Evidence for structural differences in the S domain of L in comparison with S protein of hepatitis B virus. J. Gen. Virol. 82: 1533-1541 [Abstract] [Full Text]  
  • Grgacic, E. V. L., Schaller, H. (2000). A Metastable Form of the Large Envelope Protein of Duck Hepatitis B Virus: Low-pH Release Results in a Transition to a Hydrophobic, Potentially Fusogenic Conformation. J. Virol. 74: 5116-5122 [Abstract] [Full Text]  
  • Lambert, C., Prange, R. (2001). Dual Topology of the Hepatitis B Virus Large Envelope Protein. DETERMINANTS INFLUENCING POST-TRANSLATIONAL PRE-S TRANSLOCATION. J. Biol. Chem. 276: 22265-22272 [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»