Evidence map›Paper›PMID 34731254›Full record

ReviewCellular and molecular life sciences : CMLS2021

Structural and functional insights into the spike protein mutations of emerging SARS-CoV-2 variants.

Deepali Gupta, Priyanka Sharma, Mandeep Singh, Mukesh Kumar, A S Ethayathulla, Punit Kaur

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed, 1 pooled it
3.2field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 1 synthesis or guideline pooled it, 58 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. ACS omega · 2023
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Deepali GuptaDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi,, Delhi, 110029, India.
Priyanka SharmaDepartment of Microbiology, All India Institute of Medical Sciences, New Delhi,, Delhi, 110029, India.
Mandeep SinghDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi,, Delhi, 110029, India.
Mukesh KumarDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi,, Delhi, 110029, India.
A S EthayathullaDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi,, Delhi, 110029, India.
Punit KaurDepartment of Biophysics, All India Institute of Medical Sciences, New Delhi,, Delhi, 110029, India. punitkaur@aiims.edu.ORCID http://orcid.org/0000-0002-7358-3716
All India Institute of Medical Sciences · IN

Funding

Indian Council of Medical Research IWYS04
6 · The paper itself

Abstract

Since the emergence of the first case of coronavirus disease 2019 (COVID-19), caused by severe acute respiratory syndrome coronavirus (SARS-CoV-2), the viral genome has constantly undergone rapid mutations for better adaptation in the host system. These newer mutations have given rise to several lineages/ variants of the virus that have resulted in high transmission and virulence rates compared to the previously circulating variants. Owing to this, the overall caseload and related mortality have tremendously increased globally to > 233 million infections and > 4.7 million deaths as of Sept. 28th, 2021. SARS-CoV-2, Spike (S) protein binds to host cells by recognizing human angiotensin-converting enzyme 2 (hACE2) receptor. The viral S protein contains S1 and S2 domains that constitute the binding and fusion machinery, respectively. Structural analysis of viral S protein reveals that the virus undergoes conformational flexibility and dynamicity to interact with the hACE2 receptor. The SARS-CoV-2 variants and mutations might be associated with affecting the conformational plasticity of S protein, potentially linked to its altered affinity, infectivity, and immunogenicity. This review focuses on the current circulating variants of SARS-CoV-2 and the structure-function analysis of key S protein mutations linked with increased affinity, higher infectivity, enhanced transmission rates, and immune escape against this infection.

Indexed as

Adaptation, PhysiologicalAngiotensin-Converting Enzyme 2COVID-19Genome, ViralHumansImmune EvasionProtein ConformationSARS-CoV-2Spike Glycoprotein, CoronavirusACE2 protein, humanAngiotensin-Converting Enzyme 2Spike Glycoprotein, Coronavirusspike protein, SARS-CoV-2LineagesSARS-CoV-2S proteinStructure-functional analysisVariant of concern (VOC)

Identifiers

PMID34731254
PMCPMC11073194
OpenAlexW3209675485

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.