Evidence map›Paper›PMID 35258772›Full record

ArticleGeroScience2022

Omicron variant (B.1.1.529) of SARS-CoV-2: understanding mutations in the genome, S-glycoprotein, and antibody-binding regions.

Manojit Bhattacharya, Ashish Ranjan Sharma, Kuldeep Dhama, Govindasamy Agoramoorthy, Chiranjib Chakraborty

Open access · bronzeAbstract read
In one paragraph

Article in GeroScience, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

41 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
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  7. Antibody-dependent enhancement of coronaviruses.International journal of biological sciences · 2025
    Review
  8. COVID-19 pandemic - Cocktail of variants, a study from Northern India.Journal of family medicine and primary care · 2024
    Article
  9. Review
  10. Article
  11. Review
  12. Dual Effects of 3-International journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review
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

5 authors at 5 institutions in 3 countries.

Manojit Bhattacharya *Department of Zoology, Fakir Mohan University, Vyasa Vihar, Balasore, 756020, Odisha, India.
Ashish Ranjan SharmaInstitute for Skeletal Aging & Orthopedic Surgery, Hallym University-Chuncheon Sacred Heart Hospital, Chuncheon-si, 24252, Gangwon-do, Republic of Korea.
Kuldeep DhamaDivision of Pathology, ICAR-Indian Veterinary Research Institute, Izatnagar, Bareilly, 243122, Uttar Pradesh, India.
Govindasamy AgoramoorthyCollege of Pharmacy and Health Care, Tajen University, Yanpu, Pingtung, 907, Taiwan.
Chiranjib Chakraborty *Department of Biotechnology, School of Life Science and Biotechnology, Adamas University, Barasat-Barrackpore Rd, Kolkata, West Bengal, 700126, India. drchiranjib@yahoo.com.ORCID 0000-0002-3958-239X
Adamas University · INFakir Mohan University · INHallym University · KRIndian Veterinary Research Institute · INTajen University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Omicron variant has been detected in nearly 150 countries. We analyzed the mutational landscape of Omicron throughout the genome, focusing the S-glycoprotein. We also evaluated mutations in the antibody-binding regions and observed some important mutations overlapping those of previous variants including N501Y, D614G, H655Y, N679K, and P681H. Various new receptor-binding domain mutations were detected, including Q493K, G496S, Q498R, S477N, G466S, N440K, and Y505H. New mutations were found in the NTD (Δ143-145, A67V, T95I, L212I, and Δ211) including one new mutation in fusion peptide (D796Y). There are several mutations in the antibody-binding region including K417N, E484A, Q493K, Q498R, N501Y, and Y505H and several near the antibody-binding region (S477N, T478K, G496S, G446S, and N440K). The impact of mutations in regions important for the affinity between spike proteins and neutralizing antibodies was evaluated. Furthermore, we examined the effect of significant antibody-binding mutations (K417N, T478K, E484A, and N501Y) on antibody affinity, stability to ACE2 interaction, and possibility of amino acid substitution. All the four mutations destabilize the antibody-binding affinity. This study reveals future directions for developing neutralizing antibodies against the Omicron variant.

Indexed as

COVID-19SARS-CoV-2Angiotensin-Converting Enzyme 2Antibodies, NeutralizingGlycoproteinsHumansMutationSpike Glycoprotein, CoronavirusAngiotensin-Converting Enzyme 2Antibodies, NeutralizingGlycoproteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Ab binding regionGenomeMutationsOmicronS-glycoprotein

Identifiers

PMID35258772
PMCPMC8902853
OpenAlexW4221127747

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.