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Gene Review

DHBVgp4  -  P-protein

Duck hepatitis B virus

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Disease relevance of DHBVgp4

  • Using in vitro-translated duck hepatitis B virus (DHBV) P protein, we probed the secondary structure of the protein-bound DHBV epsilon RNA (Depsilon) and observed a marked conformational change compared to free Depsilon RNA [1].
  • Replication initiation does not involve a nucleic acid primer; instead, the hepadnavirus P protein binds to the structured RNA encapsidation signal epsilon, from which it copies a short DNA primer that becomes covalently linked to the enzyme [1].
  • Packaging of this RNA pregenome into nucleocapsids and replication initiation depend crucially on the interaction of the reverse transcriptase, P protein, with the cis-acting, 5' end-proximal encapsidation signal epsilon [2].
  • To overcome this restriction we sought to produce larger amounts of DHBV P protein by expression in Escherichia coli, followed by complex reconstitution in RRL [3].
  • We have therefore experimentally determined the secondary structures of D epsilon and of the H epsilon-signal of heron hepatitis B virus which differs considerably from D epsilon in primary sequence yet interacts productively with DHBV P protein [4].

High impact information on DHBVgp4

  • Because P protein activity depends on cellular chaperones this complex can as yet only be generated by in vitro translation of duck hepatitis B virus P protein in rabbit reticulocyte lysate; functional interaction with its cognate RNA element Depsilon can be monitored by the covalent labeling of P protein during primer synthesis [5].
  • Using the structured RNA encapsidation signal (D(epsilon)) and the reverse transcriptase (P protein) of duck hepatitis B virus (DHBV) as an example, we devised a sensitive mapping procedure that yields accurate information on the minimal RNA sequence required for interaction with a few nanograms of an RNA-binding protein [6].
  • Genetic analysis of cis-acting signals required for viral replication implicates an RNA stem-loop structure in both RNA packaging and the initiation of reverse transcription, a process in which P protein also serves as the primer [7].
  • This assignment was confirmed by direct biochemical analysis: tryptic peptides from the DHBV P protein, 32P labelled at the priming amino acid by the initiating dGTP and additionally labelled internally by [35S]methionine, were isolated and analyzed in parallel to reference peptides synthesized chemically and 33P labelled by a tyrosine kinase [8].
  • Mutations outside the YMDD motif in the P protein can also cause DHBV resistant to Lamivudine [9].

Chemical compound and disease context of DHBVgp4

  • Box A contains an invariant bulky residue recently shown to be crucial for dNTP versus NTP discrimination in RTs and some DNA polymerases; its equivalent in DHBV P protein would be phenylalanine 451 (F451) [10].


  1. Formation of a functional hepatitis B virus replication initiation complex involves a major structural alteration in the RNA template. Beck, J., Nassal, M. Mol. Cell. Biol. (1998) [Pubmed]
  2. Sequence- and structure-specific determinants in the interaction between the RNA encapsidation signal and reverse transcriptase of avian hepatitis B viruses. Beck, J., Nassal, M. J. Virol. (1997) [Pubmed]
  3. Reconstitution of a functional duck hepatitis B virus replication initiation complex from separate reverse transcriptase domains expressed in Escherichia coli. Beck, J., Nassal, M. J. Virol. (2001) [Pubmed]
  4. Experimental confirmation of a hepatitis B virus (HBV) epsilon-like bulge-and-loop structure in avian HBV RNA encapsidation signals. Beck, J., Bartos, H., Nassal, M. Virology (1997) [Pubmed]
  5. A small 2'-OH- and base-dependent recognition element downstream of the initiation site in the RNA encapsidation signal is essential for hepatitis B virus replication initiation. Schaaf, S.G., Beck, J., Nassal, M. J. Biol. Chem. (1999) [Pubmed]
  6. A sensitive procedure for mapping the boundaries of RNA elements binding in vitro translated proteins defines a minimal hepatitis B virus encapsidation signal. Beck, J., Nassal, M. Nucleic Acids Res. (1996) [Pubmed]
  7. Site-specific RNA binding by a hepatitis B virus reverse transcriptase initiates two distinct reactions: RNA packaging and DNA synthesis. Pollack, J.R., Ganem, D. J. Virol. (1994) [Pubmed]
  8. Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription. Weber, M., Bronsema, V., Bartos, H., Bosserhoff, A., Bartenschlager, R., Schaller, H. J. Virol. (1994) [Pubmed]
  9. Mutations outside the YMDD motif in the P protein can also cause DHBV resistant to Lamivudine. He, J.Y., Zhu, Y.T., Yang, R.Y., Feng, L.L., Guo, X.B., Zhang, F.X., Chen, H.S. World J. Gastroenterol. (2005) [Pubmed]
  10. dNTP versus NTP discrimination by phenylalanine 451 in duck hepatitis B virus P protein indicates a common structure of the dNTP-binding pocket with other reverse transcriptases. Beck, J., Vogel, M., Nassal, M. Nucleic Acids Res. (2002) [Pubmed]
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