Evidence map›Paper›PMID 26808496›Full record

ArticlePloS one2016

Comparative Proteomics Reveals Important Viral-Host Interactions in HCV-Infected Human Liver Cells.

Shufeng Liu, Ting Zhao, BenBen Song, Jianhua Zhou, Tony T Wang

Open access · goldAbstract readComparative StudyValidation Study
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. 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

5 authors at 4 institutions in 1 country.

Shufeng LiuCenter for Immunology and Infectious Diseases, Bioscience Division, SRI International, Harrisonburg, Virginia, 22802, United States of America.
Ting ZhaoCollege of Pharmacy, University of Michigan, Ann Arbor, Michigan, 48109, United States of America.
BenBen SongSLS Global Technical Support, Pall Corporation, Port Washington, New York, 11050, United States of America.
Jianhua ZhouDepartment of Urology, School of Medicine, University of Pittsburgh Medical Center, Pittsburgh, Pennsylvania, 15232, United States of America.
Tony T WangCenter for Immunology and Infectious Diseases, Bioscience Division, SRI International, Harrisonburg, Virginia, 22802, United States of America.
SRI International · USPall Corporation (United States) · USUniversity of Michigan–Ann Arbor · USUniversity of Pittsburgh Medical Center · US

Funding

Tight Junction: Gate to HCV Tropism, Therapeutics and PathogenesisR01DK088787 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI STEIN, PAUL L · 2010 to 2019
$4.2M
NIDDK NIH HHS NIH R01DK088787NIDDK NIH HHS R01 DK088787
6 · The paper itself

Abstract

Hepatitis C virus (HCV) poses a global threat to public health. HCV envelop protein E2 is the major component on the virus envelope, which plays an important role in virus entry and morphogenesis. Here, for the first time, we affinity purified E2 complex formed in HCV-infected human hepatoma cells and conducted comparative mass spectrometric analyses. 85 cellular proteins and three viral proteins were successfully identified in three independent trials, among which alphafetoprotein (AFP), UDP-glucose: glycoprotein glucosyltransferase 1 (UGT1) and HCV NS4B were further validated as novel E2 binding partners. Subsequent functional characterization demonstrated that gene silencing of UGT1 in human hepatoma cell line Huh7.5.1 markedly decreased the production of infectious HCV, indicating a regulatory role of UGT1 in viral lifecycle. Domain mapping experiments showed that HCV E2-NS4B interaction requires the transmembrane domains of the two proteins. Altogether, our proteomics study has uncovered key viral and cellular factors that interact with E2 and provided new insights into our understanding of HCV infection.

Indexed as

Host-Pathogen InteractionsProteomicsalpha-FetoproteinsGlucuronosyltransferaseHEK293 CellsHepacivirusHumansLiverTandem Mass SpectrometryViral Nonstructural Proteinsalpha-FetoproteinsGlucuronosyltransferaseNS4B protein, flavivirusViral Nonstructural Proteins

Identifiers

PMID26808496
PMCPMC4726516
OpenAlexW2265006493

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.