Evidence map›Paper›PMID 21653661›Full record

ArticleJournal of virology2011

Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry.

Eden P Go, Geetha Hewawasam, Hua-Xin Liao, Haiyan Chen, Li-Hua Ping, Jeffrey A Anderson, David C Hua, Barton F Haynes, Heather Desaire

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

97 citing papers in PubMed, 119 citations in OpenAlex.

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  18. Synthetic Carbohydrate Chemistry and Translational Medicine.The Journal of organic chemistry · 2020
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37 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, USA.
Geetha Hewawasam
Hua-Xin Liao
Haiyan Chen
Li-Hua Ping
Jeffrey A Anderson
David C Hua
Barton F Haynes
Heather Desaire
University of Kansas · USDuke Medical Center · USJohns Hopkins University Center for AIDS Research

Funding

Neutralizing Antibody Induction by Centralized GenesP01AI061734 · NIAID · DUKE UNIVERSITY · PI HAYNES, BARTON F. · 2005 to 2009
$11.7M
Development of a rapid glycosylation profiling system using mass spec dataR01RR026061 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI DESAIRE, HEATHER R · 2009 to 2011
$935k
NCRR NIH HHS R01 RR026061NCRR NIH HHS R01RR026061NIAID NIH HHS P01 AI061734NIAID NIH HHS P01AI61734
6 · The paper itself

Abstract

The analysis of HIV-1 envelope carbohydrates is critical to understanding their roles in HIV-1 transmission as well as in binding of envelope to HIV-1 antibodies. However, direct analysis of protein glycosylation by glycopeptide-based mass mapping approaches involves structural simplification of proteins with the use of a protease followed by an isolation and/or enrichment step before mass analysis. The successful completion of glycosylation analysis is still a major analytical challenge due to the complexity of samples, wide dynamic range of glycopeptide concentrations, and glycosylation heterogeneity. Here, we use a novel experimental workflow that includes an up-front complete or partial enzymatic deglycosylation step before trypsin digestion to characterize the glycosylation patterns and maximize the glycosylation coverage of two recombinant HIV-1 transmitted/founder envelope oligomers derived from clade B and C viruses isolated from acute infection and expressed in 293T cells. Our results show that both transmitted/founder Envs had similar degrees of glycosylation site occupancy as well as similar glycan profiles. Compared to 293T-derived recombinant Envs from viruses isolated from chronic HIV-1, transmitted/founder Envs displayed marked differences in their glycosylation site occupancies and in their amounts of complex glycans. Our analysis reveals that the glycosylation patterns of transmitted/founder Envs from two different clades (B and C) are more similar to each other than they are to the glycosylation patterns of chronic HIV-1 Envs derived from their own clades.

Indexed as

Amino Acid Sequenceenv Gene Products, Human Immunodeficiency VirusGlycoside HydrolasesGlycosylationHEK293 CellsHIV-1HIV InfectionsHumansMass SpectrometrySequence AlignmentTrypsinenv Gene Products, Human Immunodeficiency VirusGlycoside HydrolasesTrypsin

Identifiers

PMID21653661
PMCPMC3147976
OpenAlexW2087859193

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.