Evidence map›Paper›PMID 36278694›Full record

ArticleProteomes2022

Proteomic Approach for Comparative Analysis of the Spike Protein of SARS-CoV-2 Omicron (B.1.1.529) Variant and Other Pango Lineages.

Mukul Jain, Nil Patil, Darshil Gor, Mohit Kumar Sharma, Neha Goel, Prashant Kaushik

Erratum issuedAbstract read
In one paragraph

Article in Proteomes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Mukul JainParul Institute of Applied Sciences, Parul University, Vadodara 391760, Gujarat, India.ORCID 0000-0003-3739-1247
Nil PatilParul Institute of Applied Sciences, Parul University, Vadodara 391760, Gujarat, India.ORCID 0000-0002-9941-3395
Darshil GorParul Institute of Applied Sciences, Parul University, Vadodara 391760, Gujarat, India.
Mohit Kumar SharmaSchool of Molecular Medicine, Medical University of Warsaw, ul. Żwirki i Wigury 61, 02-091 Warsaw, Poland.
Neha GoelInstitute of Biomedicine, University of Turku, 20500 Turku, Finland.
Prashant KaushikIndependent Researcher, 46022 Valencia, Spain.ORCID 0000-0002-3145-2849

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The novel SARS-CoV-2 variant, Omicron (B.1.1.529), is being testified, and the WHO has characterized Omicron as a variant of concern due to its higher transmissibility and very contagious behavior, immunization breakthrough cases. Here, the comparative proteomic study has been conducted on spike-protein, hACE2 of five lineages (α, β, δ, γ and Omicron. The docking was performed on spike protein- hACE-2 protein using HADDOCK, and PRODIGY was used to analyze the binding energy affinity using a reduced Haddock score. Followed by superimposition in different variant-based protein structures and calculated the esteem root mean square deviation (RMSD). This study reveals that Omicron was seen generating a monophyletic clade. Further, as α variant is the principal advanced strain after Wuhan SARS-CoV-2, and that is the reason it was showing the least likeness rate with the Omicron and connoting Omicron has developed of late with the extreme number of mutations. α variant has shown the highest binding affinity with hACE2, followed by β strain, and followed with γ. Omicron showed a penultimate binding relationship, while the δ variant was seen as having the least binding affinity. This proteomic basis in silico analysis of variable spike proteins of variants will impart light on the development of vaccines and the identification of mutations occurring in the upcoming variants.

Indexed as

ACE2OmicronSARS-CoV-2spike

Identifiers

PMID36278694
PMCPMC9624331

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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.