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

PLoS One. 2012;7(11):e48685. doi: 10.1371/journal.pone.0048685. Epub 2012 Nov 7.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates
  • Animals
  • Antiviral Agents / isolation & purification
  • Antiviral Agents / pharmacology*
  • Cell Line
  • Complex Mixtures / chemistry
  • Hepacivirus / drug effects*
  • Hepacivirus / enzymology
  • Hepacivirus / genetics
  • Interferon-alpha / metabolism
  • Porifera / chemistry*
  • Protease Inhibitors / isolation & purification
  • Protease Inhibitors / pharmacology*
  • Signal Transduction / drug effects
  • Viral Nonstructural Proteins / antagonists & inhibitors*
  • Virus Replication / drug effects

Substances

  • Acetates
  • Antiviral Agents
  • Complex Mixtures
  • Interferon-alpha
  • NS3 protein, hepatitis C virus
  • Protease Inhibitors
  • Viral Nonstructural Proteins
  • ethyl acetate

Grants and funding

This work was supported in part by grants-in-aid from the Ministry of Health, Labor, and Welfare (http://www.mhlw.go.jp/) and from the Ministry of Education, Culture, Sports, Science, and Technology of Japan (http://www.mext.go.jp/). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.