Evidence map›Paper›PMID 36565991›Full record

ArticleJournal of molecular biology2023

Variations within the Glycan Shield of SARS-CoV-2 Impact Viral Spike Dynamics.

Maddy L Newby, Carl A Fogarty, Joel D Allen, John Butler, Elisa Fadda, Max Crispin

Abstract read
In one paragraph

Article in Journal of molecular biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Stoichiometric insights into SARS-CoV-2 spike-ACE2 binding across variants.Computational and structural biotechnology journal · 2025
    Article
  10. Article
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  12. 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
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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

6 authors.

Maddy L NewbySchool of Biological Sciences, University of Southampton, Southampton, UK. Electronic address: https://twitter.com/Maddy_Newby.
Carl A FogartyDepartment of Chemistry and Hamilton Institute, Maynooth University, Maynooth, Kildare, Ireland. Electronic address: https://twitter.com/2016Carl.
Joel D AllenSchool of Biological Sciences, University of Southampton, Southampton, UK. Electronic address: https://twitter.com/JoelDalllen.
John ButlerSchool of Biological Sciences, University of Southampton, Southampton, UK.
Elisa FaddaDepartment of Chemistry and Hamilton Institute, Maynooth University, Maynooth, Kildare, Ireland. Electronic address: Elisa.Fadda@mu.ie.
Max CrispinSchool of Biological Sciences, University of Southampton, Southampton, UK. Electronic address: max.crispin@soton.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The emergence of SARS-CoV-2 variants alters the efficacy of existing immunity, whether arisen naturally or through vaccination. Understanding the structure of the viral spike assists in determining the impact of mutations on the antigenic surface. One class of mutation impacts glycosylation attachment sites, which have the capacity to influence the antigenic structure beyond the immediate site of attachment. Here, we compare the site-specific glycosylation of recombinant viral spike mimetics of B.1.351 (Beta), P.1 (Gamma), B.1.617.2 (Delta), B.1.1.529 (Omicron). The P.1 strain exhibits two additional N-linked glycan sites compared to the other variants analyzed and we investigate the impact of these glycans by molecular dynamics. The acquired N188 site is shown to exhibit very limited glycan maturation, consistent with limited enzyme accessibility. Structural modeling and molecular dynamics reveal that N188 is located within a cavity by the receptor binding domain, which influences the dynamics of these attachment domains. These observations suggest a mechanism whereby mutations affecting viral glycosylation sites have a structural impact across the protein surface.

Indexed as

COVID-19Immune EvasionPolysaccharidesSARS-CoV-2Virus AttachmentAntigens, SurfaceGlycosylationHumansSpike Glycoprotein, CoronavirusAntigens, SurfacePolysaccharidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2glycosylationmass spectrometrymolecular dynamicsSARS-CoV-2variant of concern

Identifiers

PMID36565991
PMCPMC9769069

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.