Evidence map›Paper›PMID 29426822›Full record

ArticleScientific reports2018

Chemical array system, a platform to identify novel hepatitis B virus entry inhibitors targeting sodium taurocholate cotransporting polypeptide.

Manabu Kaneko, Yushi Futamura, Senko Tsukuda, Yasumitsu Kondoh, Tomomi Sekine, Hiroyuki Hirano, Kento Fukano, Hirofumi Ohashi, Wakana Saso, Ryo Morishita and 11 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

11 citing papers in PubMed, 23 citations in OpenAlex.

  1. Hepatitis B and D virus entry.Nature reviews. Microbiology · 2025
    Review
  2. Hepatitis B: Model Systems and Therapeutic Approaches.Journal of immunology research · 2024
    Review
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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

21 authors at 8 institutions in 3 countries.

Manabu KanekoDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Yushi FutamuraChemical Biology Research Group, RIKEN Center for Sustainable Resource Science (CSRS), Wako, 351-0198, Japan.
Senko TsukudaDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Yasumitsu KondohChemical Biology Research Group, RIKEN Center for Sustainable Resource Science (CSRS), Wako, 351-0198, Japan.
Tomomi SekineBio-Active Compounds Discovery Research Unit, RIKEN CSRS, Wako, 351-0198, Japan.
Hiroyuki HiranoChemical Resource Development Research Unit, RIKEN CSRS, Wako, 351-0198, Japan.ORCID 0000-0002-0761-5548
Kento FukanoDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Hirofumi OhashiDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Wakana SasoDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Ryo MorishitaCellFree Sciences Co., Ltd, Matsuyama, 790-8577, Japan.
Satoko MatsunagaDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama, 236-0027, Japan.
Fumihiro KawaiDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Yokohama, 230-0045, Japan.
Akihide RyoDepartment of Microbiology, Yokohama City University Graduate School of Medicine, Yokohama, 236-0027, Japan.
Sam-Yong ParkDrug Design Laboratory, Graduate School of Medical Life Science, Yokohama City University, Yokohama, 230-0045, Japan.
Ryosuke SuzukiDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Hideki AizakiDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Naoko OhtaniDepartment of Applied Biological Sciences, Tokyo University of Science, Noda, 278-8510, Japan.
Camille SureauLaboratoire de Virologie Moléculaire, Institut National de la Transfusion Sanguine, INSERM U1134, Paris, 75015, France.
Takaji WakitaDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan.
Hiroyuki OsadaChemical Biology Research Group, RIKEN Center for Sustainable Resource Science (CSRS), Wako, 351-0198, Japan. hisyo@riken.jp.
Koichi WatashiDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, 162-8640, Japan. kwatashi@nih.go.jp.
National Institute of Infectious Diseases · JPRIKEN Center for Sustainable Resource Science · JPTokyo University of Science · JPYokohama City University · JPCellFree Sciences (Japan) · JPInserm · FRMeiji Pharmaceutical University · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Current anti-hepatitis B virus (HBV) agents including interferons and nucleos(t)ide analogs efficiently suppress HBV infection. However, as it is difficult to eliminate HBV from chronically infected liver, alternative anti-HBV agents targeting a new molecule are urgently needed. In this study, we applied a chemical array to high throughput screening of small molecules that interacted with sodium taurocholate cotransporting polypeptide (NTCP), an entry receptor for HBV. From approximately 30,000 compounds, we identified 74 candidates for NTCP interactants, and five out of these were shown to inhibit HBV infection in cell culture. One of such compound, NPD8716, a coumarin derivative, interacted with NTCP and inhibited HBV infection without causing cytotoxicity. Consistent with its NTCP interaction capacity, this compound was shown to block viral attachment to host hepatocytes. NPD8716 also prevented the infection with hepatitis D virus, but not hepatitis C virus, in agreement with NPD8716 specifically inhibiting NTCP-mediated infection. Analysis of derivative compounds showed that the anti-HBV activity of compounds was apparently correlated with the affinity to NTCP and the capacity to impair NTCP-mediated bile acid uptake. These results are the first to show that the chemical array technology represents a powerful platform to identify novel viral entry inhibitors.

Indexed as

Bile Acids and SaltsCoumarinsHepacivirusHepatitis B virusHepatitis Delta VirusHep G2 CellsHumansOrganic Anion Transporters, Sodium-DependentSymportersViral Fusion Protein InhibitorsVirus AttachmentVirus InternalizationBile Acids and SaltsCoumarinsOrganic Anion Transporters, Sodium-Dependentsodium-bile acid cotransporterSymportersViral Fusion Protein Inhibitors

Identifiers

PMID29426822
PMCPMC5807303
OpenAlexW2804202464

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.