Evidence map›Paper›PMID 32363391›Full record

ArticleGlycobiology2020

Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2.

Asif Shajahan, Nitin T Supekar, Anne S Gleinich, Parastoo Azadi

Open access · hybridAbstract read
In one paragraph

Article in Glycobiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 337 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
337citing papers in PubMed, 1 pooled it
11.4field-weighted citation impact, top 1% 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

337 citing papers in PubMed, 1 synthesis or guideline pooled it, 530 citations in OpenAlex.

  1. SARS-CoV-2 cell entry beyond the ACE2 receptor.Molecular biology reports · 2022
    Pooled it
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277 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

4 authors at 1 institution in 1 country.

Asif ShajahanComplex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
Nitin T SupekarComplex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
Anne S GleinichComplex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
Parastoo AzadiComplex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Rd, Athens, GA 30602, USA.
University of Georgia · US

Funding

Orbitrap Fusion Tribrid Mass SpectrometerS10OD018530 · OD · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2014 to 2014
$750k
NIH HHS S10 OD018530
6 · The paper itself

Abstract

The current emergence of the novel coronavirus pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) demands the development of new therapeutic strategies to prevent rapid progress of mortalities. The coronavirus spike (S) protein, which facilitates viral attachment, entry and membrane fusion is heavily glycosylated and plays a critical role in the elicitation of the host immune response. The spike protein is comprised of two protein subunits (S1 and S2), which together possess 22 potential N-glycosylation sites. Herein, we report the glycosylation mapping on spike protein subunits S1 and S2 expressed on human cells through high-resolution mass spectrometry. We have characterized the quantitative N-glycosylation profile on spike protein and interestingly, observed unexpected O-glycosylation modifications on the receptor-binding domain of spike protein subunit S1. Even though O-glycosylation has been predicted on the spike protein of SARS-CoV-2, this is the first report of experimental data for both the site of O-glycosylation and identity of the O-glycans attached on the subunit S1. Our data on the N- and O-glycosylation are strengthened by extensive manual interpretation of each glycopeptide spectra in addition to using bioinformatics tools to confirm the complexity of glycosylation in the spike protein. The elucidation of the glycan repertoire on the spike protein provides insights into the viral binding studies and more importantly, propels research toward the development of a suitable vaccine candidate.

Indexed as

Coronavirus InfectionsCOVID-19HumansPandemicsPolysaccharidesProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusPolysaccharidesSpike Glycoprotein, Coronaviruscoronavirus vaccineCOVID-19S1 S2 glycosylationSARS-CoV-2 glycosylationspike protein

Identifiers

PMID32363391
PMCPMC7239183
OpenAlexW3021183041

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.