ArticleThe Biochemical journal2006
Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assembly.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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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
17 citing papers in PubMed, 37 citations in OpenAlex.
- Hepatitis B Virus Nucleocapsid Assembly.Journal of molecular biology · 2025Review
- Protein kinase Cdc7 supports viral replication by phosphorylatingJournal of virology · 2023Article
- Pathogenicity and virulence of Hepatitis B virus.Virulence · 2022Review
- Hepatitis B virus core protein phosphorylation: Identification of the SRPK1 target sites and impact of their occupancy on RNA binding and capsid structure.PLoS pathogens · 2018Article
- Hepatocellular Carcinoma: Causes, Mechanism of Progression and Biomarkers.Current chemical genomics and translational medicine · 2018Review
- Hepatitis B virus core antigen mutations predict post-operative prognosis of patients with primary hepatocellular carcinoma.The Journal of general virology · 2017Article
- Phosphorylation of Beet black scorch virus coat protein by PKA is required for assembly and stability of virus particles.Scientific reports · 2015Article
- Phosphoacceptors threonine 162 and serines 170 and 178 within the carboxyl-terminal RRRS/T motif of the hepatitis B virus core protein make multiple contributions to hepatitis B virus replication.Journal of virology · 2014Article
- cAMP protein kinase phosphorylates the Mos1 transposase and regulates its activity: evidences from mass spectrometry and biochemical analyses.Nucleic acids research · 2014Article
- Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core protein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Phosphorylation events during viral infections provide potential therapeutic targets.Reviews in medical virology · 2012Article
- Modern biomolecular mass spectrometry and its role in studying virus structure, dynamics, and assembly.Angewandte Chemie (International ed. in English) · 2011Review
- Hepatitis B virus core protein with hot-spot mutations inhibit MxA gene transcription but has no effect on inhibition of virus replication by interferon α.Virology journal · 2010Article
- Hepatitis B virus core interacts with the host cell nucleolar protein, nucleophosmin 1.Journal of microbiology (Seoul, Korea) · 2009Article
- Hepatitis B: the virus and disease.Hepatology (Baltimore, Md.) · 2009Article
- Tumor necrosis factor activates a conserved innate antiviral response to hepatitis B virus that destabilizes nucleocapsids and reduces nuclear viral DNA.Journal of virology · 2007Article
- Enhancement of hepatitis B virus replication by the regulatory X protein in vitro and in vivo.Journal of virology · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein-protein interactions can be regulated by protein modifications such as phosphorylation. Some of the phosphorylation sites (Ser155, Ser162 and Ser170) of HBV (hepatitis B virus) Cp have been discovered and these sites are implicated in the regulation of viral genome encapsidation, capsid localization and nucleocapsid maturation. In the present report, the dimeric form of HBV Cp was phosphorylated by PKA (protein kinase A), but not by protein kinase C in vitro, and the phosphorylation of dimeric Cp facilitated HBV core assembly. Matrix-assisted laser-desorption ionization-time-of-flight analysis revealed that the HBV Cp was phosphorylated at Ser87 by PKA. This was further confirmed using a mutant HBV Cp with S87G mutation. The S87G mutation inhibited the phosphorylation and, as a result, the in vitro HBV core assembly was not facilitated by PKA. In addition, when either pCMV/FLAG-Core(WT) or pCMV/FLAG-Core(S87G) was transfected into HepG2 cells, few mutant Cps (S87G) assembled into capsids compared with the wild-type (WT) Cps, although the same level of total Cps was expressed in both cases. In conclusion, PKA facilitates HBV core assembly through phosphorylation of the HBV Cp at Ser87.
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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.