Evidence map›Paper›PMID 36918534›Full record

ArticleNature communications2023

Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein.

Valeria Calvaresi, Antoni G Wrobel, Joanna Toporowska, Dietmar Hammerschmid, Katie J Doores, Richard T Bradshaw, Ricardo B Parsons, Donald J Benton, Chloë Roustan, Eamonn Reading and 3 more

Open access · goldFull text read
In one paragraph

Article in Nature communications, 2023. 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
15.3field-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

50 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Switching Spike Plasticity Shapes ACE2 Engagement Across SARS-CoV-2 Variants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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

13 authors at 2 institutions in 1 country.

Valeria CalvaresiDepartment of Chemistry, King's College London, SE1 1DB, London, UK. valeria.clavaresi@kcl.ac.uk.ORCID 0000-0002-1756-8853
Antoni G WrobelStructural Biology of Disease Processes Laboratory, The Francis Crick Institute, NW1 1AT, London, UK. antoni.wrobel@crick.ac.uk.ORCID 0000-0002-6680-5587
Joanna ToporowskaDepartment of Chemistry, King's College London, SE1 1DB, London, UK.
Dietmar HammerschmidDepartment of Chemistry, King's College London, SE1 1DB, London, UK.ORCID 0000-0002-0210-3690
Katie J DooresDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, SE1 9RT, London, UK.ORCID 0000-0002-5507-1725
Richard T BradshawDepartment of Chemistry, King's College London, SE1 1DB, London, UK.ORCID 0000-0002-8652-4301
Ricardo B ParsonsDepartment of Chemistry, King's College London, SE1 1DB, London, UK.ORCID 0000-0002-9261-7360
Donald J BentonStructural Biology of Disease Processes Laboratory, The Francis Crick Institute, NW1 1AT, London, UK.ORCID 0000-0001-6748-9339
Chloë RoustanStructural Biology Science Technology Platform, The Francis Crick Institute, NW1 1AT, London, UK.
Eamonn ReadingDepartment of Chemistry, King's College London, SE1 1DB, London, UK.ORCID 0000-0001-8219-0052
Michael H MalimDepartment of Infectious Diseases, School of Immunology and Microbial Sciences, King's College London, SE1 9RT, London, UK.ORCID 0000-0002-7699-2064
Steve J GamblinStructural Biology of Disease Processes Laboratory, The Francis Crick Institute, NW1 1AT, London, UK.ORCID 0000-0001-5331-639X
Argyris PolitisDepartment of Chemistry, King's College London, SE1 1DB, London, UK. argyris.politis@manchester.ac.uk.ORCID 0000-0002-6658-3224
King's College London · GBThe Francis Crick Institute · GB

Funding

Cancer Research UK CC2060Medical Research Council MR/S015426/1Medical Research Council MR/W005611/1Wellcome Trust 220280/Z/20/ZWellcome Trust CC2060
6 · The paper itself

Abstract

SARS-CoV-2 spike glycoprotein mediates receptor binding and subsequent membrane fusion. It exists in a range of conformations, including a closed state unable to bind the ACE2 receptor, and an open state that does so but displays more exposed antigenic surface. Spikes of variants of concern (VOCs) acquired amino acid changes linked to increased virulence and immune evasion. Here, using HDX-MS, we identified changes in spike dynamics that we associate with the transition from closed to open conformations, to ACE2 binding, and to specific mutations in VOCs. We show that the RBD-associated subdomain plays a role in spike opening, whereas the NTD acts as a hotspot of conformational divergence of VOC spikes driving immune evasion. Alpha, beta and delta spikes assume predominantly open conformations and ACE2 binding increases the dynamics of their core helices, priming spikes for fusion. Conversely, substitutions in omicron spike lead to predominantly closed conformations, presumably enabling it to escape antibodies. At the same time, its core helices show characteristics of being pre-primed for fusion even in the absence of ACE2. These data inform on SARS-CoV-2 evolution and omicron variant emergence.

Indexed as

COVID-19Spike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2HumansMutationSARS-CoV-2Angiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID36918534
PMCPMC10013288
OpenAlexW4324138357

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read41
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.