Evidence map›Paper›PMID 34235568›Full record

ReviewAnalytical and bioanalytical chemistry2021

Glycosylation of SARS-CoV-2: structural and functional insights.

Asif Shajahan, Lauren E Pepi, Daniel S Rouhani, Christian Heiss, Parastoo Azadi

Open access · bronzeAbstract readReview
In one paragraph

Review in Analytical and bioanalytical chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
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  10. Photoionization of pyrenemethylamine-labeled oligosaccharides: a new MALDI-TOF precursor ion-type for efficient fragmentation.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Article
  11. Review
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  16. Characterization of Ssc, anJournal of bacteriology · 2024
    Article
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  19. Review
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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 1 institution in 1 country.

Asif ShajahanComplex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA.
Lauren E PepiComplex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA.
Daniel S RouhaniComplex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA.
Christian HeissComplex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA.
Parastoo AzadiComplex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA. azadi@ccrc.uga.edu.
University of Georgia · US

Funding

National Glycoscience Resource- CCRC Service and Training - NGlycoR@CCRCR24GM137782 · NIGMS · UNIVERSITY OF GEORGIA · PI Parastoo Azadi · 2020 to 2026
$5.2M
Orbitrap Fusion Tribrid Mass SpectrometerS10OD018530 · OD · UNIVERSITY OF GEORGIA · PI AZADI, PARASTOO · 2014 to 2014
$750k
NIGMS NIH HHS R24 GM137782NIGMS NIH HHS R24GM137782NIH HHS S10 OD018530NIH HHS S10OD018530
6 · The paper itself

Abstract

The COVID-19 pandemic is caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Similar to other coronaviruses, its particles are composed of four structural proteins: spike (S), envelope (E), membrane (M), and nucleocapsid (N) proteins. S, E, and M proteins are glycosylated, and the N protein is phosphorylated. The S protein is involved in the interaction with the host receptor human angiotensin-converting enzyme 2 (hACE2), which is also heavily glycosylated. Recent studies have revealed several other potential host receptors or factors that can increase or modulate the SARS-CoV-2 infection. Interestingly, most of these molecules bear carbohydrate residues. While glycans acquired by the viruses through the hijacking of the host machinery help the viruses in their infectivity, they also play roles in immune evasion or modulation. Glycans play complex roles in viral pathobiology, both on their own and in association with carrier biomolecules, such as proteins or glycosaminoglycans (GAGs). Understanding these roles in detail can help in developing suitable strategies for prevention and therapy of COVID-19. In this review, we sought to emphasize the interplay of SARS-CoV-2 glycosylated proteins and their host receptors in viral attachment, entry, replication, and infection. Moreover, the implications for future therapeutic interventions targeting these glycosylated biomolecules are also discussed in detail.

Indexed as

Angiotensin-Converting Enzyme 2Carbohydrate ConformationCOVID-19GlycosylationHumansPolysaccharidesProtein ConformationSARS-CoV-2Spike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2PolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Envelope protein glycosylationGlycosaminoglycan SARS-CoV-2Human ACE2 SARS-CoV-2Membrane protein glycosylationSARS-CoV-2 glycosylationSpike protein glycosylation

Identifiers

PMID34235568
PMCPMC8262766
OpenAlexW3181877484

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.