ArticleBMC microbiology2001
Evidence that the RNAseH activity of the duck hepatitis B virus is unable to act on exogenous substrates.
Article in BMC microbiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Efficient Inhibition of Hepatitis B Virus (HBV) Replication and cccDNA Formation by HBV Ribonuclease H Inhibitors during Infection.Antimicrobial agents and chemotherapy · 2021Article
- Mechanism of Hepatitis B Virus cccDNA Formation.Viruses · 2021Review
- Extracellular Hepatitis B Virus RNAs Are Heterogeneous in Length and Circulate as Capsid-Antibody Complexes in Addition to Virions in Chronic Hepatitis B Patients.Journal of virology · 2018Article
- Purification and enzymatic characterization of the hepatitis B virus ribonuclease H, a new target for antiviral inhibitors.Antiviral research · 2016Article
- The hepatitis B virus ribonuclease H as a drug target.Antiviral research · 2015Review
- Ultradeep pyrosequencing and molecular modeling identify key structural features of hepatitis B virus RNase H, a putative target for antiviral intervention.Journal of virology · 2014Article
- The hepatitis B virus ribonuclease H is sensitive to inhibitors of the human immunodeficiency virus ribonuclease H and integrase enzymes.PLoS pathogens · 2013Article
- Identification of an essential molecular contact point on the duck hepatitis B virus reverse transcriptase.Journal of virology · 2005Article
- Ligation with nucleic acid sequence-based amplification.The Journal of molecular diagnostics : JMDArticle
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundThe hepadnaviral reverse transcriptase can synthesize DNA on its native RNA template within viral cores but it is usually unable to synthesize DNA employing exogenous nucleic acids as a template. The mechanism of this template commitment is unknown. Here we provide evidence that the RNAseH activity of duck hepatitis B virus reverse transcriptase may also be unable to act on exogenous substrates.
resultsRNAseH assays were performed under a wide variety of conditions employing substrate RNAs of Duck Hepatitis B Virus sequence annealed to complementary DNA oligonucleotides and permeabilized intracellular viral core particles. Temperature, pH, cation type, salt concentration, substrate concentration, and the sequences of the cleavage sites were varied, and the effects of ATP and dNTPs on RNAseH activity were examined. duck hepatitis B virus RNAseH activity was not detected under any of these conditions, although E. coli or Avian Myeloblastosis Virus RNAseH activity could be detected under all conditions. Access of the RNA substrate to the enzyme within the viral cores was confirmed.
conclusionsThese results imply that the RNAseH activity of the DHBV reverse transcriptase may not be able to degrade exogenous RNA:DNA heteroduplexes, although it can degrade heteroduplexes of the same sequence generated during reverse transcription of the endogenous RNA template. Therefore, the RNAseH activity appears to be "substrate committed" in a manner similar to the template commitment observed for the DNA polymerase activity.
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