ArticleJournal of virology2010
Phosphorylation of serine 177 of the small hepatitis delta antigen regulates viral antigenomic RNA replication by interacting with the processive RNA polymerase II.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Human and pathogen-encoded circular RNAs in viral infections: insights into functions and therapeutic opportunities.Human molecular genetics · 2025Review
- Pathogenesis, prevention, and therapeutic advances in hepatitis B, C, and D.Virology journal · 2025Review
- Differential impact of hepatitis delta virus replication and expression of viral antigens on the cellular kinome profile.Cell communication and signaling : CCS · 2025Article
- Structure and nucleic acid interactions of the SProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Hepatitis D virus (HDV): investigational therapeutic agents in clinical trials.Expert opinion on investigational drugs · 2022Review
- Innate immune recognition and modulation in hepatitis D virus infection.World journal of gastroenterology · 2020Review
- Hepatitis Delta Virus histone mimicry drives the recruitment of chromatin remodelers for viral RNA replication.Nature communications · 2020Article
- Chronic hepatitis delta: A state-of-the-art review and new therapies.World journal of gastroenterology · 2019Review
- Novel hepatitis D-like agents in vertebrates and invertebrates.Virus evolution · 2019Article
- A review on hepatitis D: From virology to new therapies.Journal of advanced research · 2019Review
- Hepatitis Delta Antigen Regulates mRNA and Antigenome RNA Levels during Hepatitis Delta Virus Replication.Journal of virology · 2019Article
- Hepatitis delta: virological and clinical aspects.Virology journal · 2017Review
- Clade homogeneity and low rate of delta virus despite hyperendemicity of hepatitis B virus in Ethiopia.Virology journal · 2017Article
- Hepatitis delta virus: A fascinating and neglected pathogen.World journal of virology · 2015Review
- Therapeutic Strategies and New Intervention Points in Chronic Hepatitis Delta Virus Infection.International journal of molecular sciences · 2015Review
- Protein-peptide arrays for detection of specific anti-hepatitis D virus (HDV) genotype 1, 6, and 8 antibodies among HDV-infected patients by surface plasmon resonance imaging.Journal of clinical microbiology · 2015Article
- Hepatitis D virus infection, replication and cross-talk with the hepatitis B virus.World journal of gastroenterology · 2014Article
- Life cycle and pathogenesis of hepatitis D virus: A review.World journal of hepatology · 2013Review
- Hepatitis delta virus: a peculiar virus.Advances in virology · 2013Review
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent studies revealed that posttranslational modifications (e.g., phosphorylation and methylation) of the small hepatitis delta antigen (SHDAg) are required for hepatitis delta virus (HDV) replication from antigenomic to genomic RNA. The phosphorylation of SHDAg at serine 177 (Ser(177)) is involved in this step, and this residue is crucial for interaction with RNA polymerase II (RNAP II), the enzyme assumed to be responsible for antigenomic RNA replication. This study demonstrated that SHDAg dephosphorylated at Ser(177) interacted preferentially with hypophosphorylated RNAP II (RNAP IIA), which generally binds at the transcription initiation sites. In contrast, the Ser(177)-phosphorylated counterpart (pSer(177)-SHDAg) exhibited preferential binding to hyperphosphorylated RNAP II (RNAP IIO). In addition, RNAP IIO associated with pSer(177)-SHDAg was hyperphosphorylated at both the Ser(2) and Ser(5) residues of its carboxyl-terminal domain (CTD), which is a hallmark of the transcription elongation isoform. Moreover, the RNAP II CTD kinase inhibitor 5,6-dichloro-1-beta-D-ribofuranosyl-benzimidazole (DRB) not only blocked the interaction between pSer(177)-SHDAg and RNAP IIO but also inhibited HDV antigenomic RNA replication. Our results suggest that the phosphorylation of SHDAg at Ser177 shifted its affinitytoward the RNAP IIO isoform [corrected] and thus is a switch for HDV antigenomic RNA replication from the initiation to the elongation stage.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.