Evidence map›Paper›PMID 21735466›Full record

ArticleHepatology (Baltimore, Md.)2011

Hepatitis C virus E1 envelope glycoprotein interacts with apolipoproteins in facilitating entry into hepatocytes.

Budhaditya Mazumdar, Arup Banerjee, Keith Meyer, Ranjit Ray

Open access · greenAbstract readComparative Study
In one paragraph

Article in Hepatology (Baltimore, Md.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

47 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Apolipoprotein E and viral infection: Risks and Mechanisms.Molecular therapy. Nucleic acids · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. The impact of direct-acting antiviral treatment on lipid metabolism and insulin resistance in chronic hepatitis C patients: temporary? permanent?The Turkish journal of gastroenterology : the official journal of Turkish Society of Gastroenterology · 2020
    Article
  13. Hepatitis C Virus Structure: Defined by What It Is Not.Cold Spring Harbor perspectives in medicine · 2020
    Review
  14. Article
  15. Article
  16. Inhibiting PCSK9 - biology beyond LDL control.Nature reviews. Endocrinology · 2018
    Review
  17. Article
  18. Review
  19. Review
  20. Review
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

4 authors at 1 institution in 1 country.

Budhaditya MazumdarDepartment of Internal Medicine, St. Louis University, St. Louis, MO, USA.
Arup Banerjee
Keith Meyer
Ranjit Ray
Saint Louis University · US

Funding

QUALITATIVE NATURE OF ANTIBODIES TO HCV GLYCOPROTEIN SUBUNIT VACCINE IN HUMANSR01AI068769 · NIAID · SAINT LOUIS UNIVERSITY · PI RAY, RANJIT · 2006 to 2009
$1.3M
NIAID NIH HHS R01 AI068769
6 · The paper itself

Abstract

unlabelledOur previous studies demonstrated that hepatitis C virus (HCV) envelope glycoproteins 1 and 2 (E1 and E2) display distinct reactivity to different cell-surface molecules. In this study, we characterized the interaction of E1 and E2 with apolipoproteins in facilitating virus entry. The results suggested a higher neutralization of vesicular stomatitis virus (VSV)/HCV E1-G pseudotype infectivity by antibodies to apolipoprotein E (ApoE) than apolipoprotein B (ApoB), with VSV/HCV E2-G pseudotype infectivity remaining largely unaffected. Neutralization of cell-culture-grown HCV infectivity by antiserum to ApoE and, to a lesser extent, by ApoB further verified their involvement in virus entry. HCV E1, but not E2, displayed binding with ApoE and ApoB by enzyme-linked immunosorbent assay. Binding of E1 with apolipoproteins were further supported by coimmunoprecipitation from human hepatocytes expressing E1. Rabbit antiserum to a selected E1 ectodomain-derived peptide displayed ∼ 50% neutralization of E1-G pseudotype infectivity. Furthermore, E1 ectodomain-derived synthetic peptides significantly inhibited the interaction of E1 with both the apolipoproteins. Investigation on the role of low-density lipoprotein receptor (LDL-R) as a hepatocyte surface receptor for virus entry suggested a significant reduction in E1-G pseudotype plaque numbers (∼ 70%) by inhibiting LDL-R ligand-binding activity using human proprotein convertase subtilisin/kexin type 9 and platelet factor-4, whereas they had a minimal inhibitory effect on the E2-G pseudotype.

conclusionTogether, the results suggested an association between HCV E1 and apolipoproteins, which may facilitate virus entry through LDL-R into mammalian cells.

Indexed as

AnimalsApolipoproteinsCells, CulturedEnzyme-Linked Immunosorbent AssayHepacivirusHepatocytesHumansLow Density Lipoprotein Receptor-Related Protein-1Platelet Factor 4Proprotein Convertase 9Proprotein ConvertasesRabbitsSensitivity and SpecificitySerine EndopeptidasesVesicular stomatitis Indiana virusViral Envelope ProteinsApolipoproteinsE1 protein, Hepatitis C virusLow Density Lipoprotein Receptor-Related Protein-1PCSK9 protein, humanPlatelet Factor 4Proprotein Convertase 9Proprotein ConvertasesSerine EndopeptidasesViral Envelope Proteins

Identifiers

PMID21735466
PMCPMC3184191
OpenAlexW1988761191

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.