Evidence map›Paper›PMID 30651366›Full record

ArticleJournal of virology2019

Antigenicity and Immunogenicity of Differentially Glycosylated Hepatitis C Virus E2 Envelope Proteins Expressed in Mammalian and Insect Cells.

Richard A Urbanowicz, Ruixue Wang, John E Schiel, Zhen-Yong Keck, Melissa C Kerzic, Patrick Lau, Sneha Rangarajan, Kyle J Garagusi, Lei Tan, Johnathan D Guest and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

46 citing papers in PubMed, 80 citations in OpenAlex.

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  11. The red algaProceedings of the National Academy of Sciences of the United States of America · 2024
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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

15 authors at 4 institutions in 2 countries.

Richard A Urbanowicz *School of Life Sciences, The University of Nottingham, Nottingham, United Kingdom.ORCID 0000-0002-2461-4993
Ruixue Wang *W. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
John E SchielUniversity of Maryland Institute for Bioscience and Biotechnology Research, National Institute of Standards and Technology, Rockville, Maryland, USA.
Zhen-Yong KeckDepartment of Pathology, Stanford University School of Medicine, Stanford, California, USA.
Melissa C KerzicW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
Patrick LauDepartment of Pathology, Stanford University School of Medicine, Stanford, California, USA.
Sneha RangarajanW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
Kyle J GaragusiW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
Lei TanDepartment of Pathology, Stanford University School of Medicine, Stanford, California, USA.
Johnathan D GuestW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
Jonathan K BallSchool of Life Sciences, The University of Nottingham, Nottingham, United Kingdom.
Brian G PierceW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
Roy A MariuzzaW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA.
Steven K H FoungDepartment of Pathology, Stanford University School of Medicine, Stanford, California, USA.
Thomas R FuerstW. M. Keck Laboratory for Structural Biology, University of Maryland Institute for Bioscience and Biotechnology Research, Rockville, Maryland, USA tfuerst@umd.edu.
Advanced Bioscience Laboratories (United States) · USStanford University · USNottingham University Hospitals NHS Trust · GBNational Institute of Standards and Technology · US

Funding

Structure-Based Vaccine Design for Hepatits C VirusR01AI132213 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI ANDRIANOV, ALEXANDER, FOUNG, STEVEN · 2017 to 2021
$6.0M
Project 2 - FranceU19AI123862 · NIAID · STANFORD UNIVERSITY · PI FOUNG, STEVEN · 2016 to 2020
$3.9M
Graduate Training in VirologyT32AI125186 · NIAID · UNIV OF MARYLAND, COLLEGE PARK · PI SIMON, ANNE ELIZABETH · 2016 to 2020
$1.3M
Structure-based HCV vaccine designR21AI126582 · NIAID · STANFORD UNIVERSITY · PI FOUNG, STEVEN, MARIUZZA, ROY A · 2016 to 2017
$440k
Medical Research Council G0801169NIAID NIH HHS R01 AI132213NIAID NIH HHS R21 AI126582NIAID NIH HHS T32 AI125186NIAID NIH HHS U19 AI123862
6 · The paper itself

Abstract

The development of a prophylactic vaccine for hepatitis C virus (HCV) remains a global health challenge. Cumulative evidence supports the importance of antibodies targeting the HCV E2 envelope glycoprotein to facilitate viral clearance. However, a significant challenge for a B cell-based vaccine is focusing the immune response on conserved E2 epitopes capable of eliciting neutralizing antibodies not associated with viral escape. We hypothesized that glycosylation might influence the antigenicity and immunogenicity of E2. Accordingly, we performed head-to-head molecular, antigenic, and immunogenic comparisons of soluble E2 (sE2) produced in (i) mammalian (HEK293) cells, which confer mostly complex- and high-mannose-type glycans; and (ii) insect (Sf9) cells, which impart mainly paucimannose-type glycans. Mass spectrometry demonstrated that all 11 predicted

Indexed as

AnimalsAntibodies, NeutralizingAntibody FormationCell LineEpitopesFemaleGlycosylationHEK293 CellsHepacivirusHepatitis CHepatitis C AntibodiesHumansInsectaMammalsMicePolysaccharidesAntibodies, NeutralizingEpitopesglycoprotein E2, Hepatitis C virusHepatitis C AntibodiesPolysaccharidesViral Envelope Proteinsenvelope glycoproteinsHCVhepatitis C virusimmunogenicityinsect cellsmammalian cellsneutralizationvaccine

Identifiers

PMID30651366
PMCPMC6430559
OpenAlexW2909652038

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.