Evidence map›Paper›PMID 23144928›Full record

ArticlePloS one2012

Inhibition of both protease and helicase activities of hepatitis C virus NS3 by an ethyl acetate extract of marine sponge Amphimedon sp.

Yuusuke Fujimoto, Kazi Abdus Salam, Atsushi Furuta, Yasuyoshi Matsuda, Osamu Fujita, Hidenori Tani, Masanori Ikeda, Nobuyuki Kato, Naoya Sakamoto, Shinya Maekawa and 11 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
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 9 institutions in 2 countries.

Yuusuke FujimotoDepartment of Microbiology, Division of Medicine, Graduate School of Medicine and Engineering, University of Yamanashi, Yamanashi, Japan.
Kazi Abdus Salam
Atsushi Furuta
Yasuyoshi Matsuda
Osamu Fujita
Hidenori Tani
Masanori Ikeda
Nobuyuki Kato
Naoya Sakamoto
Shinya Maekawa
Nobuyuki Enomoto
Nicole J de Voogd
Masamichi Nakakoshi
Masayoshi Tsubuki
Yuji Sekiguchi
Satoshi Tsuneda
Nobuyoshi Akimitsu
Naohiro Noda
Atsuya Yamashita
Junichi Tanaka
Kohji Moriishi
National Institute of Advanced Industrial Science and Technology · JPUniversity of Yamanashi · JPHoshi University · JPJapan Radioisotope Association · JPOkayama University · JPWaseda University · JPHokkaido University · JPNaturalis Biodiversity Center · NLUniversity of the Ryukyus · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Combination therapy with ribavirin, interferon, and viral protease inhibitors could be expected to elicit a high level of sustained virologic response in patients infected with hepatitis C virus (HCV). However, several severe side effects of this combination therapy have been encountered in clinical trials. In order to develop more effective and safer anti-HCV compounds, we employed the replicon systems derived from several strains of HCV to screen 84 extracts from 54 organisms that were gathered from the sea surrounding Okinawa Prefecture, Japan. The ethyl acetate-soluble extract that was prepared from marine sponge Amphimedon sp. showed the highest inhibitory effect on viral replication, with EC₅₀ values of 1.5 and 24.9 µg/ml in sub-genomic replicon cell lines derived from genotypes 1b and 2a, respectively. But the extract had no effect on interferon-inducing signaling or cytotoxicity. Treatment with the extract inhibited virus production by 30% relative to the control in the JFH1-Huh7 cell culture system. The in vitro enzymological assays revealed that treatment with the extract suppressed both helicase and protease activities of NS3 with IC₅₀ values of 18.9 and 10.9 µg/ml, respectively. Treatment with the extract of Amphimedon sp. inhibited RNA-binding ability but not ATPase activity. These results suggest that the novel compound(s) included in Amphimedon sp. can target the protease and helicase activities of HCV NS3.

Indexed as

AcetatesAnimalsAntiviral AgentsCell LineComplex MixturesDEAD-box RNA HelicasesHepacivirusInterferon-alphaNucleoside-TriphosphatasePoriferaProtease InhibitorsSerine EndopeptidasesSignal TransductionViral Nonstructural ProteinsViral ProteasesVirus ReplicationAcetatesAntiviral AgentsComplex MixturesDEAD-box RNA Helicasesethyl acetateInterferon-alphaNS3 protein, hepatitis C virusNucleoside-TriphosphataseProtease InhibitorsSerine EndopeptidasesViral Nonstructural ProteinsViral Proteases

Identifiers

PMID23144928
PMCPMC3492463
OpenAlexW2134622266

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.