Evidence map›Paper›PMID 18330979›Full record

ArticleJournal of proteome research2008

Glycosylation site-specific analysis of HIV envelope proteins (JR-FL and CON-S) reveals major differences in glycosylation site occupancy, glycoform profiles, and antigenic epitopes' accessibility.

Eden P Go, Janet Irungu, Ying Zhang, Dilusha S Dalpathado, Hua-Xin Liao, Laura L Sutherland, S Munir Alam, Barton F Haynes, Heather Desaire

Abstract read
In one paragraph

Article in Journal of proteome research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
3.5field-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

95 citing papers in PubMed, 138 citations in OpenAlex.

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  12. Stable, high yield expression of gp145 Env glycoprotein from HIV-1 in mammalian cells.Biologicals : journal of the International Association of Biological Standardization · 2021
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35 more citing papers are in PubMed but not listed here.

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

9 authors at 3 institutions in 1 country.

Eden P GoDepartment of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA.
Janet Irungu
Ying Zhang
Dilusha S Dalpathado
Hua-Xin Liao
Laura L Sutherland
S Munir Alam
Barton F Haynes
Heather Desaire
Duke Medical Center · USUniversity of Kansas · USDuke University Hospital · US

Funding

Neutralizing Antibody Induction by Centralized GenesP01AI061734 · NIAID · DUKE UNIVERSITY · PI HAYNES, BARTON F. · 2005 to 2009
$11.7M
Comparative Glycomics of the HIV Protein gp 120R01GM077226 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI DESAIRE, HEATHER R · 2005 to 2009
$1.1M
NIAID NIH HHS P01 AI061734NIAID NIH HHS P01AI61734NIGMS NIH HHS R01 GM077226NIGMS NIH HHS R01GM077226
6 · The paper itself

Abstract

The HIV-1 envelope (Env) is a key determinant in mediating viral entry and fusion to host cells and is a major target for HIV vaccine development. While Env is typically about 50% glycan by mass, glycosylation sites are known to evolve, with some glycosylation profiles presumably being more effective at facilitating neutralization escape than others. Thus, characterizing glycosylation patterns of Env and native virions and correlating glycosylation profiles with infectivity and Env immunogenicity are necessary first steps in designing effective immunogens. Herein, we describe a mass spectrometry-based strategy to determine HIV-1 Env glycosylation patterns and have compared two mammalian cell expressed recombinant Env immunogens, one a limited immunogen and one that induces cross-clade neutralizing antibodies. We have used a glycopeptide-based mass mapping approach to identify and characterize Env's glycosylation patterns by elucidating which sites are utilized and what type of glycan motif is present at each glycosylation site. Our results show that the immunogens displayed different degrees of glycosylation as well as a different characteristic set of glycan motifs. Thus, these techniques can be used to (1) define glycosylation profiles of recombinant Env proteins and Env on mature virions, (2) define specific carbohydrate moieties at each glycosylation site, and (3) determine the role of certain carbohydrates in HIV-1 infectivity and in modulation of Env immunogenicity.

Indexed as

AIDS VaccinesAmino Acid SequenceCarbohydrate SequenceChromatography, High Pressure LiquidEpitopesGlycopeptidesGlycosylationHIV Envelope Protein gp160HumansMolecular Sequence DataMolecular StructureOligosaccharides, Branched-ChainRecombinant ProteinsSpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryAIDS VaccinesEpitopesGlycopeptidesHIV Envelope Protein gp160Oligosaccharides, Branched-ChainRecombinant ProteinsTrypsin

Identifiers

PMID18330979
PMCPMC3658474
OpenAlexW2060507246

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.