Duck hepatitis B virus (DHBV) as a model for understanding hepadnavirus neutralization

  • Sylvie Chassot
  • Véronique Lambert
  • A. Kay
  • C. Trépo
  • Lucyna Cova
Conference paper
Part of the Archives of Virology Supplementum book series (ARCHIVES SUPPL, volume 8)


The role of the immune response to the human hepatitis B virus (HBV) envelope proteins in neutralization of viral infectivity has been well documented. The similarity between HBV, prototype member of the hepadnavirus family, and the closely related duck hepatitis B virus (DHBV) has allowed, use of the latter as a convenient model for the study of molecular mechanisms of HBV replication and neutralization. In this brief review, we will examine the HBV and DHBV envelope proteins and their role as targets for virus neutralization.


Neutralization Epitope Pekin Duck Duck Hepatitis Infected Duck preS Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Appel JR, Pinilla C, Niman H, Houghten R (1990) Elucidation of discontinuous linear determinants in peptides. J Immunol 144: 976–983PubMedGoogle Scholar
  2. 2.
    Budkowska A, Dubreuil P, Capel F, Pillot J (1986) Hepatitis B virus pre-S gene-encoded antigenic specificity and anti-pre-S antibody: relationship between anti-pre-S response and recovery. Hepatology 6: 360–368PubMedCrossRefGoogle Scholar
  3. 3.
    Büscher M, Reiser W, Will H, Schaller H (1985) Transcripts and the putative RNA pregenome of duck hepatitis B virus: implications for reverse transcription. Cell 40: 717–724PubMedCrossRefGoogle Scholar
  4. 4.
    Chassot S, Lambert V, Kay A, Godinot C, Roux B, Trepo C, Cova L (1993) Fine mapping of neutralization epitopes on duck hepatitis B virus (DHBV) pre-S protein using monoclonal antibodies and overlapping octapeptides. Virology 192: 217–223PubMedCrossRefGoogle Scholar
  5. 5.
    Cheung RC, Robinson WS, Marion PL, Greenberg HB (1989) Epitope mapping of neutralizing monoclonal antibodies against duck hepatitis B virus. J Virol 63: 2445–2451PubMedGoogle Scholar
  6. 6.
    Cheung RC, Trujillo DE, Robinson WS, Greenberg HB, Marion PL (1990) Epitope-specific antibody response to the surface antigen of duck hepatitis B virus in infected ducks. Virology 176: 546–552PubMedCrossRefGoogle Scholar
  7. 7.
    Emini EA, Larson V, Eichberg J, Conard P, Garsky VM, Lee DR, Ellis RW, Miller WJ, Anderson CA, Gerety RJ (1989) Protective effect of a synthetic peptide comprising the complete preS2 region of the hepatitis B virus surface protein. J Med Virol 28: 7–12PubMedCrossRefGoogle Scholar
  8. 8.
    Ganem D, Varmus HE (1987) The molecular biology of the hepatitis B viruses. Annu Rev Biochem 56: 651–693PubMedCrossRefGoogle Scholar
  9. 9.
    Gust ID, Burreil CJ, Coulepis AG, Robinson WS, Zuckerman AJ (1986) Taxonomic classification of human hepatitis B virus. Intervirology 25: 14–29PubMedCrossRefGoogle Scholar
  10. 10.
    Heermann KH, Kruse F, Seifer M, Gerlich WH (1987) Immunogenicity of the gene S and pre-S domains in hepatitis B virions and HBsAg filaments. Intervirology 28: 14–25PubMedCrossRefGoogle Scholar
  11. 11.
    Itoh Y, Takai E, Ohnuma H, Kitajima K, Tsuda F, Machida A, Mishiro S, Nakamura T, Miyakawa Y, Mayumi M (1986) A synthetic peptide vaccine involving the product of the preS(2) region of hepatitis B virus DNA: protective efficacity in chimpanzees. Proc Natl Acad Sci USA 83: 9174–9178PubMedCrossRefGoogle Scholar
  12. 12.
    Klingmüller U, Schaller H (1992) A highly conserved region in the pre-S domain of the duck hepatitis B virus is essential for binding and infection: implications from in vitro binding data that the DHBV receptor is a complex molecular biology of hepatitis B viruses. In: Chiseri FV, Gowans EJ (eds) Molecular biology of hepatitis B viruses, abstracts. University of California Press, San Diego, p 53Google Scholar
  13. 13.
    Klinkert MQ, Theilmann L, Pfaff E, Schaller H (1986) Pre-S1 antigens and antibodies early in the course of acute hepatitis B virus infection. J Virol 58: 522–525PubMedGoogle Scholar
  14. 14.
    Lambert V, Fernholz D, Sprengel R, Fourel I, Deleage G, Wildner G, Peyret C, Trepo C, Cova L, Will H (1990) Virus-neutralizing monoclonal antibody to a conserved epitope on the duck hepatitis B virus pre-S protein. J Virol 64: 1290–1297PubMedGoogle Scholar
  15. 15.
    Lambert V, Chassot S, Kay A, Trepo C, Cova L (1991) In vivo neutralization of duck hepatitis B virus by antibodies specific to the N-terminal portion of pre-S protein. Virology 185: 446–450PubMedCrossRefGoogle Scholar
  16. 16.
    Li JS, Cova L, Buckland R, Lambert V, Deléage G, Trépo C (1989) Duck hepatitis B virus can tolerate insertion, deletion and partial frameshift mutation in the distal pre-S region. J Virol 63: 4965–4968PubMedGoogle Scholar
  17. 17.
    Macrae DR, Bruss V, Ganem D (1991) Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly. Virology 181: 359–363PubMedCrossRefGoogle Scholar
  18. 18.
    Marion PL, Knight SS, Feitelson MA, Oshiro LS, Robinson WS (1983) Major polypeptide of duck hepatitis B surface antigen particles. J Virol 48: 534–541PubMedGoogle Scholar
  19. 19.
    Neurath AR, Kent SBH, Strick N, Parker K (1986) Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus. Cell 46: 429–436PubMedCrossRefGoogle Scholar
  20. 20.
    Neurath AR, Seto B, Strick N (1989) Antibodies to synthetic peptides from the preS1 region of the hepatitis B virus (HBV) envelope (env) protein are virus-neutralizing and protective. Vaccine 7: 234–236PubMedCrossRefGoogle Scholar
  21. 21.
    Neurath AR, Thanavala Y (1990) Hepadnaviruses. In: Regenmortel MHV, Neurath AR (eds) Immunochemistry of viruses, vol 2: The basis of serodiagnosis and vaccines. Elsevier, Amsterdam, pp 403–458Google Scholar
  22. 22.
    Persing DH, Varmus HE, Ganem D (1987) The preS1 protein of hepatitis B virus is acetylated at its amino terminus with myristic acid. J Virol 61: 1672–1677PubMedGoogle Scholar
  23. 23.
    Pugh JC, Sninsky JJ, Summers JW, Schaeffer E (1987) Characterization of a pre-S polypeptide on the surfaces of infectious avian hepadnavirus particles. J Virol 61: 1384–1390PubMedGoogle Scholar
  24. 24.
    Schlicht HJ, Kuhn C, Guhr B, Mattaliano RJ, Schaller H (1987) Biochemical and immunological characterization of the duck hepatitis B virus envelope proteins. J Virol 61: 2280–2285PubMedGoogle Scholar
  25. 25.
    Schödel F, Sprengel R, Weimer T, Fernholz D, Schneider R, Will H (1989) Animal hepatitis B viruses. Adv Viral Oncol 8: 73–102Google Scholar
  26. 26.
    Schödel F, Weimer T, Fernholz D, Schneider R, Sprengel R, Wildner G, Will H (1991) The biology of avian hepatitis B viruses. In: McLachlan A (ed) Molecular biology of the hepatitis B virus. CRC Press, Boca Raton, pp 53–80Google Scholar
  27. 27.
    Theilmann L, Burkhard HD, Galle PR, Gmelin K, Kommerell B, Pfaff E (1988) Detection of antibodies against pre-S1 proteins in sera of patients with hepatitis B virus infection by ELISA using a pre-S fusion protein expressed in E. coli. Drug Res 38: 1856–1858Google Scholar
  28. 28.
    Vickery K, Freiman JS, Dixon RJ, Kearney R, Murray S, Cossart YE (1989) Immunity in Pekin ducks experimentally and naturally infected with duck hepatitis B virus. J Med Virol 28: 231–236PubMedCrossRefGoogle Scholar
  29. 29.
    Yokosuka O, Omata M, Ito Y (1988) Expression of pre-S1, pre-S2, and C proteins in duck hepatitis B virus infection. Virology 167: 82–86PubMedCrossRefGoogle Scholar
  30. 30.
    Yuasa S, Cheung RC, Pham Q, Robinson WS, Marion PL (1991) Peptide mapping of neutralizing and nonneutralizing epitopes of duck hepatitis B virus pre-S polypeptide. Virology 181: 14–21PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag 1993

Authors and Affiliations

  • Sylvie Chassot
    • 1
  • Véronique Lambert
    • 1
  • A. Kay
    • 2
  • C. Trépo
    • 1
  • Lucyna Cova
    • 1
  1. 1.INSERM U 271LyonFrance
  2. 2.Centre Hayem, Hôpital Saint-LouisUPR 41-CNRSParisFrance

Personalised recommendations