Evidence map›Paper›PMID 32818519›Full record

ReviewAntiviral research2020

Targeting the multifunctional HBV core protein as a potential cure for chronic hepatitis B.

Usha Viswanathan, Nagraj Mani, Zhanying Hu, Haiqun Ban, Yanming Du, Jin Hu, Jinhong Chang, Ju-Tao Guo

Open access · greenAbstract readReview
In one paragraph

Review in Antiviral research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
8.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 97 citations in OpenAlex.

  1. Trial
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  9. Anticodon Engineered Transfer RNA (tRNAAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
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5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Usha ViswanathanBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA.
Nagraj ManiArbutus Biopharma Inc., 701 Veterans Circle, Warminster, PA, 18974, USA.
Zhanying HuBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA.
Haiqun BanBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA.
Yanming DuBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA.
Jin HuBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA.
Jinhong ChangBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA.
Ju-Tao GuoBaruch S. Blumberg Institute, 3805 Old Easton Road, Doylestown, PA, 18902, USA. Electronic address: ju-tao.guo@bblumberg.org.
Baruch S. Blumberg Institute · US

Funding

Evaulation of therapeutic benefits of HBV nucleocapsid assembly inhibitorsR01AI113267 · NIAID · DREXEL UNIVERSITY · PI DU, YANMING, GUO, JU-TAO · 2014 to 2018
$2.9M
NIAID NIH HHS R01 AI113267
6 · The paper itself

Abstract

The core (capsid) protein of hepatitis B virus (HBV) is the building block of nucleocapsids where viral DNA reverse transcriptional replication takes place and mediates virus-host cell interaction important for the persistence of HBV infection. The pleiotropic role of core protein (Cp) in HBV replication makes it an attractive target for antiviral therapies of chronic hepatitis B, a disease that affects more than 257 million people worldwide without a cure. Recent clinical studies indicate that core protein allosteric modulators (CpAMs) have a great promise as a key component of hepatitis B curative therapies. Particularly, it has been demonstrated that modulation of Cp dimer-dimer interactions by several chemical series of CpAMs not only inhibit nucleocapsid assembly and viral DNA replication, but also induce the disassembly of double-stranded DNA-containing nucleocapsids to prevent the synthesis of cccDNA. Moreover, the different chemotypes of CpAMs modulate Cp assembly by interaction with distinct amino acid residues at the HAP pocket between Cp dimer-dimer interfaces, which results in the assembly of Cp dimers into either non-capsid Cp polymers (type I CpAMs) or empty capsids with distinct physical property (type II CpAMs). The different CpAMs also differentially modulate Cp metabolism and subcellular distribution, which may impact cccDNA metabolism and host antiviral immune responses, the critical factors for the cure of chronic HBV infection. This review article highlights the recent research progress on the structure and function of core protein in HBV replication cycle, the mode of action of CpAMs, as well as the current status and perspectives on the discovery and development of core protein-targeting antivirals. This article forms part of a symposium in Antiviral Research on "Wide-ranging immune and direct-acting antiviral approaches to curing HBV and HDV infections."

Indexed as

Hepatitis B Core AntigensAnimalsAntiviral AgentsDNA ReplicationDNA, ViralHepatitis B, ChronicHepatitis B virusHep G2 CellsHumansMiceNucleocapsidViral Core ProteinsVirus ReplicationAntiviral AgentsDNA, ViralHepatitis B Core AntigensViral Core ProteinsCapsidcccDNACore protein allosteric modulatorsHepatitis B virusNucleocapsid

Identifiers

PMID32818519
PMCPMC8050868
OpenAlexW3075029329

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.