Evidence map›Paper›PMID 33064451›Full record

ArticleAnalytical chemistry2020

Comprehensive Analysis of the Glycan Complement of SARS-CoV-2 Spike Proteins Using Signature Ions-Triggered Electron-Transfer/Higher-Energy Collisional Dissociation (EThcD) Mass Spectrometry.

Dongxia Wang, Jakub Baudys, Jonathan L Bundy, Maria Solano, Theodore Keppel, John R Barr

Open access · hybridAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
7.9field-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

41 citing papers in PubMed, 74 citations in OpenAlex.

  1. Analytical applications of gas-phase ion chemistry enabled by mass spectrometry.Analytical methods : advancing methods and applications · 2026
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  19. Principles of SARS-CoV-2 glycosylation.Current opinion in structural biology · 2022
    Review
  20. Characterization of a SARS-CoV-2 spike protein reference material.Analytical and bioanalytical chemistry · 2022
    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

6 authors at 1 institution in 1 country.

Dongxia WangDivision of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, 4770 Buford Highway, Northeast, Atlanta, Georgia 30341, United States.ORCID 0000-0002-0993-1018
Jakub BaudysDivision of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, 4770 Buford Highway, Northeast, Atlanta, Georgia 30341, United States.
Jonathan L BundyDivision of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, 4770 Buford Highway, Northeast, Atlanta, Georgia 30341, United States.
Maria SolanoDivision of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, 4770 Buford Highway, Northeast, Atlanta, Georgia 30341, United States.ORCID 0000-0002-7853-3523
Theodore KeppelDivision of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, 4770 Buford Highway, Northeast, Atlanta, Georgia 30341, United States.
John R BarrDivision of Laboratory Sciences, National Center for Environmental Health, Centers for Disease Control and Prevention, 4770 Buford Highway, Northeast, Atlanta, Georgia 30341, United States.
Centers for Disease Control and Prevention · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has led to a global pandemic of coronavirus disease 2019 (COVID-19). The spike protein expressed on the surface of this virus is highly glycosylated and plays an essential role during the process of infection. We conducted a comprehensive mass spectrometric analysis of the N-glycosylation profiles of the SARS-CoV-2 spike proteins using signature ions-triggered electron-transfer/higher-energy collision dissociation (EThcD) mass spectrometry. The patterns of N-glycosylation within the recombinant ectodomain and S1 subunit of the SARS-CoV-2 spike protein were characterized using this approach. Significant variations were observed in the distribution of glycan types as well as the specific individual glycans on the modification sites of the ectodomain and subunit proteins. The relative abundance of sialylated glycans in the S1 subunit compared to the full-length protein could indicate differences in the global structure and function of these two species. In addition, we compared N-glycan profiles of the recombinant spike proteins produced from different expression systems, including human embryonic kidney (HEK 293) cells and

Indexed as

AnimalsBetacoronavirusGlycosylationHEK293 CellsHumansMass SpectrometryPolysaccharidesSARS-CoV-2Spike Glycoprotein, CoronavirusSpodopteraPolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID33064451
PMCPMC7586457
OpenAlexW3092658851

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.