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Gene Review

DHBVgp6  -  pre-S protein

Duck hepatitis B virus

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Disease relevance of DHBVgp6

  • The duck hepatitis B virus model system was used to elucidate the characteristics of receptor (carboxypeptidase D, gp180) interaction with polypeptides representing the receptor binding site in the preS part of the large viral surface protein [1].
  • We found that amino acids 201 to 205 of the pre-S envelope protein of woodchuck hepatitis virus (WHV) form a conserved amino acid cluster, Gly-Asp-Pro-Ala-Leu (GDPAL), which resembles the DDPLL sequence of DHBV [2].
  • Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor [3].
  • Thus, the pre-S region is exposed on the surfaces of infectious virions and may be directly involved in binding of virus to host-cell receptors [4].
  • Avian hepatitis B virus infection is initiated by the interaction of a distinct pre-S subdomain with the cellular receptor gp180 [5].

High impact information on DHBVgp6

  • The most effective antisense oligodeoxynucleotide was directed against the 5' region of the pre-S gene and resulted in a complete inhibition of viral replication and gene expression in vitro and in vivo [6].
  • A single amino acid change of glycine to glutamic acid at position 133 (G133E) in the preS protein of duck hepatitis B virus (DHBV) caused an increase in the intranuclear pool of viral covalently closed circular DNA (cccDNA), resulting in a transient elevation of viral replication and eventual hepatocyte destruction [7].
  • We found that an in-frame deletion of this small region inhibited virion formation, suggesting that the GDPAL region of the pre-S envelope protein was required for virus assembly and/or secretion of WHV [2].
  • Unfortunately, ganciclovir therapy did not substantially affect CCC DNA or viral RNA levels, and the treatment resulted in an increase in the intrahepatic expression of the viral envelope proteins, pre-S and S [8].
  • The DGD protein expressed in rabbit reticulocyte lysates bound truncated DHBV pre-S protein identical to that of p120 derived from duck liver confirming DGD as p120 [9].

Chemical compound and disease context of DHBVgp6


Biological context of DHBVgp6


Anatomical context of DHBVgp6


Associations of DHBVgp6 with chemical compounds

  • Using metabolic labelling with 32P and digestion with residue-specific phosphatases, we demonstrate that L protein heterogeneity is due to phosphorylation of threonine and/or serine residues within the pre-S domain [15].
  • After only two in vivo neutralization rounds with Mab 900, five different pre-S mutant genomes were identified, which harbored point mutations affecting only proline residues located at position 90 within this epitope (83IPQPQWTP90) and/or at a distance at position 5 [18].

Other interactions of DHBVgp6


Analytical, diagnostic and therapeutic context of DHBVgp6

  • Combining results from surface plasmon resonance spectroscopy and two-dimensional NMR analysis we resolved the contribution of preS sequence elements to complex stability and show that receptor binding potentially occurs in two steps [1].
  • Western-blot analysis for the production of viral pre-S/S proteins revealed a marked stimulation of viral protein synthesis in hypertonic media, whereas hypotonic exposure inhibited it [20].
  • All pre-S/S and S-vaccinated ducks developed total anti-DHBs and specific anti-S antibodies with similar titers reaching 1/10,000 to 1/50,000 and 1/2,500 to 1/4,000, respectively, after the third vaccination [16].
  • For mapping of the epitope, polypeptides from different regions of the DHBV pre-S/S gene were expressed in Escherichia coli and used as the substrate for immunoblotting [21].
  • After the viral genome was cloned and sequenced, a comparative sequence analysis revealed an identical genome organization of HHBV and DHBV (pre-C/C-, pre-S/S-, and pol-ORFs) [22].


  1. Receptor recognition by a hepatitis B virus reveals a novel mode of high affinity virus-receptor interaction. Urban, S., Schwarz, C., Marx, U.C., Zentgraf, H., Schaller, H., Multhaup, G. EMBO J. (2000) [Pubmed]
  2. The GDPAL region of the pre-S1 envelope protein is important for morphogenesis of woodchuck hepatitis virus. Yu, M., Emerson, S.U., Cote, P., Shapiro, M., Purcell, R.H. Hepatology (1998) [Pubmed]
  3. Hepadnavirus infection requires interaction between the viral pre-S domain and a specific hepatocellular receptor. Klingmüller, U., Schaller, H. J. Virol. (1993) [Pubmed]
  4. Characterization of a pre-S polypeptide on the surfaces of infectious avian hepadnavirus particles. Pugh, J.C., Sninsky, J.J., Summers, J.W., Schaeffer, E. J. Virol. (1987) [Pubmed]
  5. Avian hepatitis B virus infection is initiated by the interaction of a distinct pre-S subdomain with the cellular receptor gp180. Urban, S., Breiner, K.M., Fehler, F., Klingmüller, U., Schaller, H. J. Virol. (1998) [Pubmed]
  6. In vivo inhibition of duck hepatitis B virus replication and gene expression by phosphorothioate modified antisense oligodeoxynucleotides. Offensperger, W.B., Offensperger, S., Walter, E., Teubner, K., Igloi, G., Blum, H.E., Gerok, W. EMBO J. (1993) [Pubmed]
  7. Acute liver injury following infection with a cytopathic strain of duck hepatitis B virus. Lenhoff, R.J., Luscombe, C.A., Summers, J. Hepatology (1999) [Pubmed]
  8. Long-term ganciclovir chemotherapy for congenital duck hepatitis B virus infection in vivo: effect on intrahepatic-viral DNA, RNA, and protein expression. Luscombe, C., Pedersen, J., Uren, E., Locarnini, S. Hepatology (1996) [Pubmed]
  9. Identification and expression of glycine decarboxylase (p120) as a duck hepatitis B virus pre-S envelope-binding protein. Li, J., Tong, S., Wands, J.R. J. Biol. Chem. (1999) [Pubmed]
  10. Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection. Tong, S., Li, J., Wands, J.R. J. Virol. (1995) [Pubmed]
  11. Phosphorylation of DHBV pre-S: identification of the major site of phosphorylation and effects of mutations on the virus life cycle. Borel, C., Sunyach, C., Hantz, O., Trepo, C., Kay, A. Virology (1998) [Pubmed]
  12. Analysis of the binding of a host cell surface glycoprotein to the preS protein of duck hepatitis B virus. Ishikawa, T., Kuroki, K., Lenhoff, R., Summers, J., Ganem, D. Virology (1994) [Pubmed]
  13. Duck hepatitis B virus can tolerate insertion, deletion, and partial frameshift mutation in the distal pre-S region. Li, J.S., Cova, L., Buckland, R., Lambert, V., Deléage, G., Trépo, C. J. Virol. (1989) [Pubmed]
  14. Host cell-virus cross talk: phosphorylation of a hepatitis B virus envelope protein mediates intracellular signaling. Rothmann, K., Schnölzer, M., Radziwill, G., Hildt, E., Moelling, K., Schaller, H. J. Virol. (1998) [Pubmed]
  15. The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domain. Grgacic, E.V., Anderson, D.A. J. Virol. (1994) [Pubmed]
  16. Protective efficacy of DNA vaccines against duck hepatitis B virus infection. Triyatni, M., Jilbert, A.R., Qiao, M., Miller, D.S., Burrell, C.J. J. Virol. (1998) [Pubmed]
  17. Dual topology of the large envelope protein of duck hepatitis B virus: determinants preventing pre-S translocation and glycosylation. Swameye, I., Schaller, H. J. Virol. (1997) [Pubmed]
  18. In vivo selection of duck hepatitis B virus pre-S variants which escape from neutralization. Sunyach, C., Chassot, S., Jamard, C., Kay, A., Trepo, C., Cova, L. Virology (1997) [Pubmed]
  19. Characterization of infectious and defective cloned avian hepadnavirus genomes. Wildner, G., Fernholz, D., Sprengel, R., Schneider, R., Will, H. Virology (1991) [Pubmed]
  20. Effects of anisotonic exposure on duck hepatitis B virus replication. Offensperger, W.B., Offensperger, S., Stoll, B., Gerok, W., Häussinger, D. Hepatology (1994) [Pubmed]
  21. Virus-neutralizing monoclonal antibody to a conserved epitope on the duck hepatitis B virus pre-S protein. Lambert, V., Fernholz, D., Sprengel, R., Fourel, I., Deléage, G., Wildner, G., Peyret, C., Trépo, C., Cova, L., Will, H. J. Virol. (1990) [Pubmed]
  22. Isolation and characterization of a hepatitis B virus endemic in herons. Sprengel, R., Kaleta, E.F., Will, H. J. Virol. (1988) [Pubmed]
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