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 Vietheer, P. T. K.
Right arrow Articles by Bartholomeusz, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vietheer, P. T. K.
Right arrow Articles by Bartholomeusz, A.

 Previous Article

Journal of Virology, May 2005, p. 6570-6573, Vol. 79, No. 10
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.10.6570-6573.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Failure of the Lamivudine-Resistant rtM204I Hepatitis B Virus Mutants To Efficiently Support Hepatitis Delta Virus Secretion

P. T. K. Vietheer,1 H. J. Netter,1 T. Sozzi,2 and A. Bartholomeusz2*

Department of Microbiology, Monash University, Clayton, VIC 3800,1 Victorian Infectious Disease Reference Laboratory, North Melbourne, VIC 3051, Australia2

Received 26 August 2004/ Accepted 14 January 2005

Hepatitis delta virus (HDV) is encapsidated by the envelope proteins of hepatitis B virus (HBV). The major HBV lamivudine (LMV)-resistant mutations in the polymerase gene within the reverse transcriptase (rt) region at rtM204V or rtM204I are associated with changes in the overlapping envelope gene products, in particular, the gene encoding small envelope protein (s) at sI195M or sW196L/S/Stop. We have demonstrated that the LMV resistance mutations corresponding to sW196L/S inhibited secretion of HDV particles, while changes corresponding to sI195M did not affect secretion. Differential efficiencies of HBsAg proteins expressed by LMV-resistant HBV to support HDV secretion may have consequences for clinical prognosis as coinfected patients are treated with antiviral agents.

* Corresponding author. Mailing address: Victorian Infectious Diseases Reference Laboratory, 10 Wreckyn St., North Melbourne, Vic 3051, Australia. Phone: 61 3 9342 2604. Fax: 61 3 9342 2666. E-mail: angeline{at}mh.org.au.

Journal of Virology, May 2005, p. 6570-6573, Vol. 79, No. 10
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.10.6570-6573.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Blanchet, M., Sureau, C. (2006). Analysis of the Cytosolic Domains of the Hepatitis B Virus Envelope Proteins for Their Function in Viral Particle Assembly and Infectivity. J. Virol. 80: 11935-11945 [Abstract] [Full Text]  
  • Komla-Soukha, I., Sureau, C. (2006). A tryptophan-rich motif in the carboxyl terminus of the small envelope protein of hepatitis B virus is central to the assembly of hepatitis delta virus particles.. J. Virol. 80: 4648-4655 [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»