Evidence map›Paper›PMID 35126971›Full record

ArticleChemical science2022

Fine-tuning the spike: role of the nature and topology of the glycan shield in the structure and dynamics of the SARS-CoV-2 S.

Aoife M Harbison, Carl A Fogarty, Toan K Phung, Akash Satheesan, Benjamin L Schulz, Elisa Fadda

Abstract read
In one paragraph

Article in Chemical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
–field-weighted citation impact
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

50 citing papers in PubMed.

  1. Article
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  5. Molecular mechanisms of RaTG13 and SARS-CoV-2 RBD bound to Rhinolophus affinis bat ACE2.Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. The accomplices: Heparan sulfates and N-glycans foster SARS-CoV-2 spike:ACE2 receptor binding and virus priming.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Article
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  20. Review
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.

Aoife M HarbisonDepartment of Chemistry and Hamilton Institute, Maynooth University Maynooth Kildare Ireland elisa.fadda@mu.ie.
Carl A FogartyDepartment of Chemistry and Hamilton Institute, Maynooth University Maynooth Kildare Ireland elisa.fadda@mu.ie.
Toan K PhungSchool of Chemistry and Molecular Biosciences, The University of Queensland St Lucia QLD Australia.
Akash SatheesanDepartment of Chemistry and Hamilton Institute, Maynooth University Maynooth Kildare Ireland elisa.fadda@mu.ie.
Benjamin L SchulzSchool of Chemistry and Molecular Biosciences, The University of Queensland St Lucia QLD Australia.ORCID https://orcid.org/0000-0002-4823-7758
Elisa FaddaDepartment of Chemistry and Hamilton Institute, Maynooth University Maynooth Kildare Ireland elisa.fadda@mu.ie.ORCID https://orcid.org/0000-0002-2898-7770

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dense glycan shield is an essential feature of the SARS-CoV-2 spike (S) architecture, key to immune evasion and to the activation of the prefusion conformation. Recent studies indicate that the occupancy and structures of the SARS-CoV-2 S glycans depend not only on the nature of the host cell, but also on the structural stability of the trimer; a point that raises important questions about the relative competence of different glycoforms. Moreover, the functional role of the glycan shield in the SARS-CoV-2 pathogenesis suggests that the evolution of the sites of glycosylation is potentially intertwined with the evolution of the protein sequence to affect optimal activity. Our results from multi-microsecond molecular dynamics simulations indicate that the type of glycosylation at N234, N165 and N343 greatly affects the stability of the receptor binding domain (RBD) open conformation, and thus its exposure and accessibility. Furthermore, our results suggest that the loss of glycosylation at N370, a newly acquired modification in the SARS-CoV-2 S glycan shield's topology, may have contributed to increase the SARS-CoV-2 infectivity as we find that

Identifiers

PMID35126971
PMCPMC8729800

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Registered trials

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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.