Evidence map›Paper›PMID 22660965›Full record

ArticleGlycoconjugate journal2012

Specific interaction of the envelope glycoproteins E1 and E2 with liver heparan sulfate involved in the tissue tropismatic infection by hepatitis C virus.

Fumi Kobayashi, Shuhei Yamada, Shuhei Taguwa, Chikako Kataoka, Satomi Naito, Yoshiki Hama, Hideki Tani, Yoshiharu Matsuura, Kazuyuki Sugahara

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Sulfated motifs in heparan sulfate inhibitProteoglycan research · 2023
    Article
  5. Review
  6. Relevance of Rab Proteins for the Life Cycle of Hepatitis C Virus.Frontiers in cell and developmental biology · 2018
    Review
  7. Article
  8. Glycosaminoglycans and infection.Frontiers in bioscience (Landmark edition) · 2016
    Review
  9. Proteoglycans in liver cancer.World journal of gastroenterology · 2016
    Review
  10. Article
  11. Review
  12. Role of glycosaminoglycans in infectious disease.Methods in molecular biology (Clifton, N.J.) · 2015
    Article
  13. Article
  14. 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

9 authors at 3 institutions in 1 country.

Fumi KobayashiLaboratory of Proteoglycan Signaling and Therapeutics, Hokkaido University Graduate School of Life Science, West-11, North-21, Kita-ku, Sapporo, 001-0021, Japan.
Shuhei Yamada
Shuhei Taguwa
Chikako Kataoka
Satomi Naito
Yoshiki Hama
Hideki Tani
Yoshiharu Matsuura
Kazuyuki Sugahara
Osaka University · JPKobe Pharmaceutical University · JPHokkaido University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The first step in the process of infections by the hepatitis C virus (HCV) is attachment to the host cell, which is assumed to be mediated by interaction of the envelope glycoproteins E1 and E2 with cell surface glycosaminoglycans. In this study, a variety of glycosaminoglycans, heparan sulfate (HS) from various bovine tissues as well as chondroitin sulfate (CS)/dermatan sulfate from bovine liver, were used to examine the direct interaction with recombinant E1 and E2 proteins. Intriguingly, among HS preparations from various bovine tissues, only liver HS strongly bound to both E1 and E2. Since HS from liver, which is the target tissue of HCV, contains highly sulfated structures compared to HS from other tissues, the present results suggest that HS-proteoglycan on the liver cell surface appears to be one of the molecules that define the liver-specific tissue tropism of HCV infection. The interaction assay with chemically modified heparin derivatives provided evidence that the binding of the viral proteins to heparin/HS is not only mediated by simple ionic interactions, but that the 6-O-sulfation and N-sulfation are important. Heparin oligosaccharides equal to or larger than 10-mer were required to inhibit the binding. Notably, a highly sulfated CS-E preparation from squid cartilage also strongly interacted with both viral proteins and inhibited the entry of pseudotype HCV into the target cells, suggesting that the highly sulfated CS-E might be useful as an anti-HCV drug.

Indexed as

AnimalsBinding SitesCattleCell LineHepacivirusHeparan SulfateLiverViral Envelope ProteinsE1 protein, Hepatitis C virusglycoprotein E2, Hepatitis C virusHeparan SulfateViral Envelope Proteins

Identifiers

PMID22660965
OpenAlexW1976978514

What OpenQuestion holds

Textmetadata
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.