Evidence map›Paper›PMID 36465857›Full record

ArticleiScience2023

Conformational stability of SARS-CoV-2 glycoprotein spike variants.

Hiam R S Arruda, Tulio M Lima, Renata G F Alvim, Fernanda B A Victorio, Daniel P B Abreu, Federico F Marsili, Karen D Cruz, Mayra A Marques, Patricia Sosa-Acosta, Mauricio Quinones-Vega and 5 more

Open access · goldAbstract read
In one paragraph

Article in iScience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
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

15 authors at 2 institutions in 1 country.

Hiam R S ArrudaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
Tulio M LimaCell Culture Engineering Laboratory, COPPE, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-598, Brazil.
Renata G F AlvimCell Culture Engineering Laboratory, COPPE, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-598, Brazil.
Fernanda B A VictorioCell Culture Engineering Laboratory, COPPE, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-598, Brazil.
Daniel P B AbreuCell Culture Engineering Laboratory, COPPE, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-598, Brazil.
Federico F MarsiliCell Culture Engineering Laboratory, COPPE, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-598, Brazil.
Karen D CruzInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
Mayra A MarquesInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
Patricia Sosa-AcostaBiochemistry Program, Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-909, Brazil.
Mauricio Quinones-VegaBiochemistry Program, Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-909, Brazil.
Jéssica de S GuedesBiochemistry Program, Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-909, Brazil.
Fábio C S NogueiraBiochemistry Program, Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-909, Brazil.
Jerson L SilvaInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
Leda R CastilhoCell Culture Engineering Laboratory, COPPE, Federal University of Rio de Janeiro (UFRJ), Rio de Janeiro, RJ 21941-598, Brazil.
Guilherme A P de OliveiraInstitute of Medical Biochemistry Leopoldo de Meis, National Institute of Science and Technology for Structural Biology and Bioimaging, National Center of Nuclear Magnetic Resonance Jiri Jonas, Federal University of Rio de Janeiro, Rio de Janeiro, RJ 21941-902, Brazil.
Universidade Federal do Rio de Janeiro · BRNational Institute of Science and Technology for Structural Biology and Bioimaging · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The severe acute respiratory syndrome spread worldwide, causing a pandemic. SARS-CoV-2 mutations have arisen in the spike, a glycoprotein at the viral envelope and an antigenic candidate for vaccines against COVID-19. Here, we present comparative data of the glycosylated full-length ancestral and D614G spike together with three other transmissible strains classified by the World Health Organization as variants of concern: beta, gamma, and delta. By showing that D614G has less hydrophobic surface exposure and trimer persistence, we place D614G with features that support a model of temporary fitness advantage for virus spillover. Furthermore, during the SARS-CoV-2 adaptation, the spike accumulates alterations leading to less structural stability for some variants. The decreased trimer stability of the ancestral and gamma and the presence of D614G uncoupled conformations mean higher ACE-2 affinities compared to the beta and delta strains. Mapping the energetics and flexibility of variants is necessary to improve vaccine development.

Indexed as

BiochemistryProtein structure aspectsStructural biologyVirology

Identifiers

PMID36465857
PMCPMC9710096
OpenAlexW4310424078

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.