Evidence map›Paper›PMID 33778179›Full record

ArticleHeliyon2021

Mutational analysis of structural proteins of SARS-CoV-2.

Shweta Jakhmola, Omkar Indari, Dharmendra Kashyap, Nidhi Varshney, Ayan Das, Elangovan Manivannan, Hem Chandra Jha

Open access · goldAbstract read
In one paragraph

Article in Heliyon, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.5field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

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  12. FRET-based hACE2 receptor mimic peptide conjugated nanoprobe for simple detection of SARS-CoV-2.Chemical engineering journal (Lausanne, Switzerland : 1996) · 2022
    Article
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  17. Heterologous immunity induced by 1Frontiers in immunology · 2022
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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

7 authors at 2 institutions in 1 country.

Shweta JakhmolaDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, India.
Omkar IndariDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, India.
Dharmendra KashyapDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, India.
Nidhi VarshneyDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, India.
Ayan DasDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, India.
Elangovan ManivannanSchool of Pharmacy, Devi Ahilya Vishwavidyalaya, Indore, India.
Hem Chandra JhaDepartment of Biosciences and Biomedical Engineering, Indian Institute of Technology Indore, Indore, India.
Indian Institute of Technology Indore · INDevi Ahilya Vishwavidyalaya · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SARS-CoV-2 transmissibility is higher than that of other human coronaviruses; therefore, it poses a threat to the populated communities. We investigated mutations among envelope (E), membrane (M), and spike (S) proteins from different isolates of SARS-CoV-2 and plausible signaling influenced by mutated virus in a host. We procured updated protein sequences from the NCBI virus database. Mutations were analyzed in the retrieved sequences of the viral proteins through multiple sequence alignment. Additionally, the data was subjected to ScanPROSITE to analyse if the mutations generated a relevant sequence for host signaling. Unique mutations in E, M, and S proteins resulted in modification sites like PKC phosphorylation and N-myristoylation sites. Based on structural analysis, our study revealed that the D614G mutation in the S protein diminished the interaction with T859 and K854 of adjacent chains. Moreover, the S protein of SARS-CoV-2 consists of an Arg-Gly-Asp (RGD) tripeptide sequence, which could potentially interact with various members of integrin family receptors. RGD sequence in S protein might aid in the initial virus attachment. We speculated crucial host pathways which the mutated isolates of SARS-CoV-2 may alter like PKC, Src, and integrin mediated signaling pathways. PKC signaling is known to influence the caveosome/raft pathway which is critical for virus entry. Additionally, the myristoylated proteins might activate NF-κB, a master molecule of inflammation. Thus the mutations may contribute to the disease pathogenesis and distinct lung pathophysiological changes. Further the frequently occurring mutations in the protein can be studied for possible therapeutic interventions.

Indexed as

D614GIntegrinMutationsSARS-CoV-2Signaling pathwaysSpike protein

Identifiers

PMID33778179
PMCPMC7980187
OpenAlexW3137935268

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.