Evidence map›Paper›PMID 27984693›Full record

ArticleACS chemical biology2017

Global N-Glycan Site Occupancy of HIV-1 gp120 by Metabolic Engineering and High-Resolution Intact Mass Spectrometry.

Weston B Struwe, Alexandra Stuckmann, Anna-Janina Behrens, Kevin Pagel, Max Crispin

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

24 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Uncovering the Role ofJournal of the American Chemical Society · 2023
    Article
  4. ACS chemical biology · 2022
    Article
  5. Review
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  7. Article
  8. Article
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  10. Article
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  13. Article
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  15. Review
  16. ProbingChemical science · 2019
    Article
  17. Article
  18. N-glycan microheterogeneity regulates interactions of plasma proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. 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 3 institutions in 3 countries.

Weston B StruweOxford Glycobiology Institute, Department of Biochemistry, University of Oxford , Oxford, OX1 3QU, United Kingdom.ORCID 0000-0003-0594-226X
Alexandra StuckmannFree University Berlin , Department of Chemistry and Biochemistry, Takustrasse 3, 14195 Berlin, Germany.
Anna-Janina BehrensOxford Glycobiology Institute, Department of Biochemistry, University of Oxford , Oxford, OX1 3QU, United Kingdom.
Kevin PagelFree University Berlin , Department of Chemistry and Biochemistry, Takustrasse 3, 14195 Berlin, Germany.
Max CrispinOxford Glycobiology Institute, Department of Biochemistry, University of Oxford , Oxford, OX1 3QU, United Kingdom.
Freie Universität Berlin · DEUniversity of Oxford · GBScripps Research Institute · US

Funding

Support Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BAROUCH, DAN H. · 2012 to 2018
$131.5M
NIAID NIH HHS UM1 AI100663
6 · The paper itself

Abstract

A vital step in HIV vaccine development strategies has been the observation that some infected individuals generate broadly neutralizing antibodies that target the glycans on the surface of HIV-1 gp120. These antibodies target glycan epitopes on viral envelope spikes, and yet the positions and degree of occupancy of glycosylation sites is diverse. Therefore, there is a need to understand glycosylation occupancy on recombinant immunogens. The sheer number of potential glycosylation sites and degree of chemical heterogeneity impedes assessing the global sequon occupancy of gp120 glycoforms. Here, we trap the glycan processing of recombinant gp120 to generate homogeneous glycoforms, facilitating occupancy assessment by intact mass spectrometry. We show that gp120 monomers of the BG505 strain contain either fully occupied sequons or missing the equivalent of one and sometimes two glycans across the molecule. This biosynthetic engineering approach enables the analysis of therapeutically important glycoproteins otherwise recalcitrant to analysis by native mass spectrometry.

Indexed as

Metabolic EngineeringBinding SitesHIV-1HIV Envelope Protein gp120Mass SpectrometryPolysaccharidesHIV Envelope Protein gp120Polysaccharides

Identifiers

PMID27984693
PMCPMC5543417
OpenAlexW2566733408

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.