Evidence map›Paper›PMID 20304457›Full record

ArticleVirology2010

Lack of complex N-glycans on HIV-1 envelope glycoproteins preserves protein conformation and entry function.

Dirk Eggink, Mark Melchers, Manfred Wuhrer, Thijs van Montfort, Antu K Dey, Benno A Naaijkens, Kathryn B David, Valentin Le Douce, André M Deelder, Kenneth Kang and 5 more

Erratum issuedAbstract read
In one paragraph

Article in Virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.6field-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

54 citing papers in PubMed, 75 citations in OpenAlex.

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  15. Hydroponic Treatment ofFrontiers in plant science · 2018
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

15 authors at 4 institutions in 2 countries.

Dirk EgginkLaboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam (CINIMA), Academic Medical Center of the University of Amsterdam, 1105 AZ Amsterdam, The Netherlands.
Mark Melchers
Manfred Wuhrer
Thijs van Montfort
Antu K Dey
Benno A Naaijkens
Kathryn B David
Valentin Le Douce
André M Deelder
Kenneth Kang
William C Olson
Ben Berkhout
Cornelis H Hokke
John P Moore
Rogier W Sanders
Amsterdam UMC Location University of Amsterdam · NLCornell University · USLeiden University Medical Center · NLProgenics Pharmaceuticals (United States) · US

Funding

Trimer Production and Immunogenicity TestingP01AI082362 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 2009 to 2014
$16.0M
NEUTRALIZATION OF PRIMARY HIV1 VIRUSESR37AI036082 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 1998 to 2017
$7.0M
Neutralization of Primate Immunodeficiency VirusesR01AI036082 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI JOHN P MOORE · 1994 to 2026
$4.3M
MODIFIED ENVELOPE GLYCOPROTEINS FOR HIV1 VACCINER01AI045463 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 1999 to 2010
$4.2M
NIAID NIH HHS AI082362NIAID NIH HHS AI36082NIAID NIH HHS AI45463NIAID NIH HHS P01 AI082362NIAID NIH HHS R01 AI036082NIAID NIH HHS R01 AI045463NIAID NIH HHS R37 AI036082
6 · The paper itself

Abstract

The HIV-1 envelope glycoprotein complex (Env) is the focus of vaccine development aimed at eliciting humoral immunity. Env's extensive and heterogeneous N-linked glycosylation affects folding, binding to lectin receptors, antigenicity and immunogenicity. We characterized recombinant Env proteins and virus particles produced in mammalian cells that lack N-acetylglucosaminyltransferase I (GnTI), an enzyme necessary for the conversion of oligomannose N-glycans to complex N-glycans. Carbohydrate analyses revealed that trimeric Env produced in GnTI(-/-) cells contained exclusively oligomannose N-glycans, with incompletely trimmed oligomannose glycans predominating. The folding and conformation of Env proteins was little affected by the manipulation of the glycosylation. Viruses produced in GnTI(-/-) cells were infectious, indicating that the conversion to complex glycans is not necessary for Env entry function, although virus binding to the C-type lectin DC-SIGN was enhanced. Manipulating Env's N-glycosylation may be useful for structural and functional studies and for vaccine design.

Indexed as

Virus InternalizationCarbohydrate SequenceCell Lineenv Gene Products, Human Immunodeficiency VirusHIV-1HumansModels, MolecularMolecular Sequence DataN-AcetylglucosaminyltransferasesPolysaccharidesProtein ConformationRecombinant ProteinsVirus Replicationalpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase Ienv Gene Products, Human Immunodeficiency VirusN-AcetylglucosaminyltransferasesPolysaccharidesRecombinant Proteins

Identifiers

PMID20304457
PMCPMC3776475
OpenAlexW2043521256

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.