Evidence map›Paper›PMID 35164561›Full record

ArticlemBio2021

SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy.

Ziwei Yang, Yang Han, Shilei Ding, Wei Shi, Tongqing Zhou, Andrés Finzi, Peter D Kwong, Walther Mothes, Maolin Lu

Abstract read
In one paragraph

Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Drugs against broad-spectrum of coronaviruses.Frontiers in immunology · 2026
    Review
  6. Article
  7. Article
  8. Article
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  13. 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

9 authors.

Ziwei Yang *Department of Microbial Pathogenesis, Yale Universitygrid.47100.32 School of Medicine, New Haven, Connecticut, USA.
Yang Han *Department of Cellular and Molecular Biology, University of Texas Health Science Center, Tyler, Texas, USA.
Shilei DingCentre de Recherche du CHUM (CRCHUM), Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montréal, Quebec, Canada.
Wei ShiVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.
Tongqing ZhouVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.ORCID 0000-0002-3935-4637
Andrés FinziCentre de Recherche du CHUM (CRCHUM), Département de Microbiologie, Infectiologie et Immunologie, Université de Montréal, Montréal, Quebec, Canada.ORCID 0000-0002-4992-5288
Peter D KwongVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Healthgrid.94365.3d, Bethesda, Maryland, USA.ORCID 0000-0003-3560-232X
Walther MothesDepartment of Microbial Pathogenesis, Yale Universitygrid.47100.32 School of Medicine, New Haven, Connecticut, USA.ORCID 0000-0002-3367-7240
Maolin LuDepartment of Cellular and Molecular Biology, University of Texas Health Science Center, Tyler, Texas, USA.ORCID 0000-0002-8099-6447

Funding

Structure and Dynamics of the SARS-CoV-2 Spike ProteinR01AI163395 · NIAID · YALE UNIVERSITY · PI MOTHES, WALTHER H · 2021 to 2025
$4.1M
NIAID NIH HHS R01 AI163395
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants of concern (VOCs) harbor mutations in the spike (S) glycoprotein that confer more efficient transmission and dampen the efficacy of COVID-19 vaccines and antibody therapies. S mediates virus entry and is the primary target for antibody responses, with structural studies of soluble S variants revealing an increased propensity toward conformations accessible to the human angiotensin-converting enzyme 2 (hACE2) receptor. However, real-time observations of conformational dynamics that govern the structural equilibriums of the S variants have been lacking. Here, we report single-molecule Förster resonance energy transfer (smFRET) studies of critical mutations observed in VOCs, including D614G and E484K, in the context of virus particles. Investigated variants predominately occupied more open hACE2-accessible conformations, agreeing with previous structures of soluble trimers. Additionally, these S variants exhibited slower transitions in hACE2-accessible/bound states. Our finding of increased S kinetic stability in the open conformation provides a new perspective on SARS-CoV-2 adaptation to the human population.

Indexed as

COVID-19SARS-CoV-2Biological EvolutionCOVID-19 VaccinesHumansProtein BindingProtein ConformationReceptors, VirusSpike Glycoprotein, CoronavirusCOVID-19 VaccinesReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2conformational dynamicsSARS-CoV-2 variantssingle-molecule FRETspike glycoproteinstructure

Identifiers

PMID35164561
PMCPMC8844933

What OpenQuestion holds

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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.