Evidence map›Paper›PMID 17257269›Full record

ArticleCellular microbiology2007

Core protein domains involved in hepatitis C virus-like particle assembly and budding at the endoplasmic reticulum membrane.

Christophe Hourioux, Malika Ait-Goughoulte, Romuald Patient, Delphine Fouquenet, Fabienne Arcanger-Doudet, Denys Brand, Annette Martin, Philippe Roingeard

Open access · bronzeAbstract read
In one paragraph

Article in Cellular microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Review
  3. Emerging role of lipophagy in liver disorders.Molecular and cellular biochemistry · 2024
    Review
  4. Article
  5. Review
  6. Activation of the CaViruses · 2022
    Article
  7. Viroporins: Structure, function, and their role in the life cycle of SARS-CoV-2.The international journal of biochemistry & cell biology · 2022
    Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Hepatitis C virus: assembly and release of virus particles.The Journal of biological chemistry · 2010
    Review
  19. Article
  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

8 authors at 1 institution in 1 country.

Christophe HouriouxUniversité François Rabelais de Tours, INSERM ERI 19 Tours, France.
Malika Ait-Goughoulte
Romuald Patient
Delphine Fouquenet
Fabienne Arcanger-Doudet
Denys Brand
Annette Martin
Philippe Roingeard
Institut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatitis C virus (HCV) core protein, expressed with a Semliki forest virus (SFV) replicon, self-assembles into HCV-like particles (HCV-LPs) at the endoplasmic reticulum (ER) membrane, providing an opportunity to study HCV particle morphogenesis by electron microscopy. Various mutated HCV core proteins with engineered internal deletions were expressed with this system, to identify core domains required or dispensable for HCV-LP assembly. The HCV core protein sequence was compared with its counterpart in GB virus B (GBV-B), the virus most closely related to HCV, to identify conserved domains. GBV-B and HCV display similar tropism for liver hepatocytes and their core proteins are organized similarly into three main domains (I, II and III), although GBV-B core is smaller and lacks approximately 35 amino acids (aa) in domain I. The deletion of short hydrophobic domains (aa 133-152 and 153-167 in HCV core) that appear highly conserved in domain II of both GBV-B and HCV core proteins resulted in loss of HCV core ER anchoring and self-assembly into HCV-LPs. The deletion of short domains found within domain I of HCV core protein but not in the corresponding domain of GBV-B core according to sequence alignment had contrasting effects. Amino acids 15-28 and 60-66 were shown to be dispensable for HCV-LP assembly and morphogenesis, whereas aa 88-106 were required for this process. The production of GBV-B core protein from a recombinant SFV vector was associated with specific ER ultrastructural changes, but did not lead to the morphogenesis of GBV-B-LPs, suggesting that different budding mechanisms occur in members of the Flaviviridae family.

Indexed as

Amino Acid SequenceAnimalsBlotting, WesternCell LineEndoplasmic ReticulumGB virus BHepacivirusHydrophobic and Hydrophilic InteractionsMicroscopy, ConfocalMicroscopy, Electron, TransmissionMolecular Sequence DataMutationSequence DeletionSequence Homology, Amino AcidViral Core ProteinsViral Core Proteins

Identifiers

PMID17257269
PMCPMC2216084
OpenAlexW2091663135

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.