Evidence map›Paper›PMID 37064465›Full record

ArticleHeliyon2023

Structural insights into the effect of mutations in the spike protein of SARS-CoV-2 on the binding with human furin protein.

Muhammad Suleman, Muhammad Luqman, Dong-Qing Wei, Shahid Ali, Syed Shujait Ali, Abbas Khan, Haji Khan, Zafar Ali, Wajid Khan, Muhammad Rizwan and 1 more

Open access · goldAbstract read
In one paragraph

Article in Heliyon, 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
2.1field-weighted citation impact, top 13% 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, 11 citations in OpenAlex.

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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

11 authors at 2 institutions in 2 countries.

Muhammad SulemanCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Muhammad LuqmanCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Dong-Qing WeiCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Shahid AliCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Syed Shujait AliCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Abbas KhanDepartment of Bioinformatics and Biological Statistics, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, PR China.
Haji KhanCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Zafar AliCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Wajid KhanCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Muhammad RizwanCenter for Biotechnology and Microbiology, University of Swat, Swat, Pakistan.
Naeem UllahDepartment of Computer and Software Technology, University of Swat, Swat, Pakistan.
University of Swat · PKShanghai Jiao Tong University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SARS COV-2 and its variants are spreading around the world at an alarming speed, due to its higher transmissibility and the conformational changes caused by mutations. The resulting COVID-19 pandemic has imposed severe health consequences on human health. Several countries of the world including Pakistan have studied its genome extensively and provided productive findings. In the current study, the mCSM, DynaMut2, and I-Mutant servers were used to analyze the effect of identified mutations on the structural stability of spike protein however, the molecular docking and simulations approaches were used to evaluate the dynamics of the bonding network between the wild-type and mutant spike proteins with furin. We addressed the mutational modifications that have occurred in the spike protein of SARS-COV-2 that were found in 215 Pakistani's isolates of COVID-19 patients to study the influence of mutations on the stability of the protein and its interaction with the host cell. We found 7 single amino acid substitute mutations in various domains that reside in spike protein. The H49Y, N74K, G181V, and G446V were found in the S1 domain while the D614A, V622F, and Q677H mutations were found in the central helices of the spike protein. Based on the observation, G181V, G446V, D614A, and V622F mutants were found highly destabilizing and responsible for structural perturbation. Protein-protein docking and molecular simulation analysis with that of furin have predicted that all the mutants enhanced the binding efficiency however, the V622F mutant has greatly altered the binding capacity which is further verified by the K

Indexed as

FurinMolecular dockingMolecular simulationMutationSARS COV-2S-Protein

Identifiers

PMID37064465
PMCPMC10065812
OpenAlexW4362466430

What OpenQuestion 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 OpenQuestion graph.