Literature DB >> 9188604

Insertions within epsilon affect synthesis of minus-strand DNA before the template switch for duck hepatitis B virus.

H Jiang1, D D Loeb.   

Abstract

Duck hepatitis B virus (DHBV) is a DNA virus that replicates via reverse transcription of a pregenomic RNA (pgRNA). Synthesis of the first strand of DNA (minus-strand DNA) for DHBV can be divided into two steps: (i) synthesis of the first four nucleotides of minus-strand DNA, which is primed by the viral polymerase (P) protein and copied from the sequence 5'-UUAC-3' within the phylogenetically conserved bulge in the encapsidation signal (epsilon) near the 5' end of pgRNA; and (ii) a template switch of the four-nucleotide minus-strand DNA from epsilon to an acceptor site near the 3' end of pgRNA and synthesis of a complete minus-strand DNA. To understand why only four nucleotides of minus-strand DNA were synthesized before the template switch, we introduced small insertions immediately 5' to the UUAC sequence in epsilon and determined whether these epsilon variants were competent for protein priming and whether minus strands longer than four nucleotides were synthesized. Then we determined, in cell culture, whether the longer minus-strand DNAs were competent to undergo a template switch. Also, we analyzed the structure of the epsilon variants, in solution. We found that the epsilon variants were functional for protein priming and RNA encapsidation and that the insertions were copied into minus-strand DNA. However, two mutant viruses that contained two different three-nucleotide insertions failed to synthesize minus-strand DNA efficiently from the acceptor site, even though seven nucleotides of the donor and acceptor sites were identical. These results suggest that the length and/or sequence of the minus-strand DNA copied from epsilon can be important for an efficient template switch. The RNA structural analysis of the epsilon variants indicated alteration in the position and size of the bulge. Overall, these results are consistent with the notion that the template within epsilon is limited to four nucleotides because the remaining two nucleotides located within the bulge are inaccessible for polymerization.

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Year:  1997        PMID: 9188604      PMCID: PMC191772          DOI: 10.1128/JVI.71.7.5345-5354.1997

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  36 in total

1.  The reverse transcriptase of hepatitis B virus acts as a protein primer for viral DNA synthesis.

Authors:  G H Wang; C Seeger
Journal:  Cell       Date:  1992-11-13       Impact factor: 41.582

2.  cis-acting sequences required for encapsidation of duck hepatitis B virus pregenomic RNA.

Authors:  R C Hirsch; D D Loeb; J R Pollack; D Ganem
Journal:  J Virol       Date:  1991-06       Impact factor: 5.103

Review 3.  Viral DNA synthesis.

Authors:  C Seeger; J Summers; W S Mason
Journal:  Curr Top Microbiol Immunol       Date:  1991       Impact factor: 4.291

4.  Expression of functional hepatitis B virus polymerase in yeast reveals it to be the sole viral protein required for correct initiation of reverse transcription.

Authors:  J E Tavis; D Ganem
Journal:  Proc Natl Acad Sci U S A       Date:  1993-05-01       Impact factor: 11.205

5.  Two regions of an avian hepadnavirus RNA pregenome are required in cis for encapsidation.

Authors:  J Calvert; J Summers
Journal:  J Virol       Date:  1994-04       Impact factor: 5.103

6.  Reverse transcription in hepatitis B viruses is primed by a tyrosine residue of the polymerase.

Authors:  F Zoulim; C Seeger
Journal:  J Virol       Date:  1994-01       Impact factor: 5.103

7.  Novel mechanism for reverse transcription in hepatitis B viruses.

Authors:  G H Wang; C Seeger
Journal:  J Virol       Date:  1993-11       Impact factor: 5.103

8.  An RNA stem-loop structure directs hepatitis B virus genomic RNA encapsidation.

Authors:  J R Pollack; D Ganem
Journal:  J Virol       Date:  1993-06       Impact factor: 5.103

9.  The encapsidation signal on the hepatitis B virus RNA pregenome forms a stem-loop structure that is critical for its function.

Authors:  T Knaus; M Nassal
Journal:  Nucleic Acids Res       Date:  1993-08-25       Impact factor: 16.971

10.  Hepadnavirus P protein utilizes a tyrosine residue in the TP domain to prime reverse transcription.

Authors:  M Weber; V Bronsema; H Bartos; A Bosserhoff; R Bartenschlager; H Schaller
Journal:  J Virol       Date:  1994-05       Impact factor: 5.103

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  3 in total

1.  A high level of mutation tolerance in the multifunctional sequence encoding the RNA encapsidation signal of an avian hepatitis B virus and slow evolution rate revealed by in vivo infection.

Authors:  Bernadette Schmid; Christine Rösler; Michael Nassal
Journal:  J Virol       Date:  2011-07-13       Impact factor: 5.103

2.  Complementarity between epsilon and phi sequences in pregenomic RNA influences hepatitis B virus replication efficiency.

Authors:  Claudia E Oropeza; Alan McLachlan
Journal:  Virology       Date:  2006-10-23       Impact factor: 3.616

3.  A Tyr residue in the reverse transcriptase domain can mimic the protein-priming Tyr residue in the terminal protein domain of a hepadnavirus P protein.

Authors:  Jürgen Beck; Michael Nassal
Journal:  J Virol       Date:  2011-05-18       Impact factor: 5.103

  3 in total

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