Evidence map›Paper›PMID 23946462›Full record

ArticleJournal of virology2013

Efficiency of E2-p7 processing modulates production of infectious hepatitis C virus.

Saravanabalaji Shanmugam, MinKyung Yi

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. AlphaFold Prediction of Protein-Protein Interactions in theInternational journal of molecular sciences · 2025
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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

2 authors at 1 institution in 1 country.

Saravanabalaji ShanmugamDepartment of Microbiology and Immunology, University of Texas Medical Branch at Galveston, Galveston, Texas, USA.
MinKyung Yi
The University of Texas Medical Branch at Galveston · US

Funding

Function of NS2 in Hepatitis C Virus Assembly and ReleaseR01AI075090 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI YI, MINKYUNG · 2008 to 2012
$1.6M
NIAID NIH HHS R01 AI075090
6 · The paper itself

Abstract

Previous studies indicate that the processing of hepatitis C virus (HCV) E2-p7-NS2 precursor mediated by host signal peptidase is relatively inefficient, resulting in the accumulation of E2-p7-NS2 and E2-p7 precursors in addition to E2 in mammalian cells. In this study, we discovered that a significant inhibition of the processing at an E2-p7 junction site is detrimental for HCV production, whether it was caused by the mutations in p7 or by the strategic introduction of a mutation at a terminal residue of E2 to block the signal peptidase-mediated cleavage of this junction site. However, complete separation of E2 and p7 by inserting an encephalomyocarditis virus (EMCV) internal ribosome entry site (IRES) between these two proteins also moderately inhibited virus production. These results indicate that optimal processing of the E2-p7 junction site is critical for efficient HCV production. We further demonstrated that disrupting E2-p7 processing inhibits both NS2 localization to the putative virus assembly sites near lipid droplets (LD) and NS2 interaction with NS3 and E2. However, the impact, if any, of the p7-NS2 processing efficiency on HCV production seems relatively minor. In conclusion, these results imply that effective release of E2 and p7 from the precursor E2-p7 promotes HCV production by enhancing NS2-associated virus assembly complex formation near LD.

Indexed as

Protein Processing, Post-TranslationalVirus ReplicationCell LineHepacivirusHepatocytesHumansProtein PrecursorsViral Envelope ProteinsViral Nonstructural ProteinsViral ProteinsViroporin ProteinsVirus Assemblyglycoprotein E2, Hepatitis C virusNS2 protein, Hepatitis C virusp7 protein, Hepatitis C virusProtein PrecursorsViral Envelope ProteinsViral Nonstructural ProteinsViral ProteinsViroporin Proteins

Identifiers

PMID23946462
PMCPMC3807289
OpenAlexW2105142495

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.