Evidence map›Paper›PMID 34043733›Full record

ArticlePloS one2021

Molecular dynamics analysis of N-acetyl-D-glucosamine against specific SARS-CoV-2's pathogenicity factors.

Ömür Baysal, Naeem Abdul Ghafoor, Ragıp Soner Silme, Alexander N Ignatov, Volha Kniazeva

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 13 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

5 authors at 4 institutions in 3 countries.

Ömür BaysalFaculty of Science, Department of Molecular Biology and Genetics, Molecular Microbiology Unit, Muğla Sıtkı Koçman University, Menteşe-Muğla, Turkey.ORCID 0000-0001-5104-0983
Naeem Abdul GhafoorFaculty of Science, Department of Molecular Biology and Genetics, Molecular Microbiology Unit, Muğla Sıtkı Koçman University, Menteşe-Muğla, Turkey.ORCID 0000-0002-4200-7679
Ragıp Soner SilmeCenter for Research and Practice in Biotechnology and Genetic Engineering, Istanbul University, Istanbul, Turkey.ORCID 0000-0001-6547-3747
Alexander N IgnatovFederal State Autonomous Educational Institution, People's Friendship University of Russia, Moscow, Russia.ORCID 0000-0003-2948-753X
Volha KniazevaInstitute of Biophysics and Cell Engineering of the National Academy of Sciences of Belarus, Minsk, Belarus.
Muğla University · TRIstanbul University · TRNational Academy of Sciences of Belarus · BYPeoples' Friendship University of Russia · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The causative agent of the pandemic identified as SARS-CoV-2 leads to a severe respiratory illness similar to SARS and MERS with fever, cough, and shortness of breath symptoms and severe cases that can often be fatal. In our study, we report our findings based on molecular docking analysis which could be the new effective way for controlling the SARS-CoV-2 virus and additionally, another manipulative possibilities involving the mimicking of immune system as occurred during the bacterial cell recognition system. For this purpose, we performed molecular docking using computational biology techniques on several SARS-CoV-2 proteins that are responsible for its pathogenicity against N-acetyl-D-glucosamine. A similar molecular dynamics analysis has been carried out on both SARS-CoV-2 and anti-Staphylococcus aureus neutralizing antibodies to establish the potential of N-acetyl-D-glucosamine which likely induces the immune response against the virus. The results of molecular dynamic analysis have confirmed that SARS-CoV-2 spike receptor-binding domain (PDB: 6M0J), RNA-binding domain of nucleocapsid phosphoprotein (PDB: 6WKP), refusion SARS-CoV-2 S ectodomain trimer (PDB: 6X79), and main protease 3clpro at room temperature (PDB: 7JVZ) could bind with N-acetyl-D-glucosamine that these proteins play an important role in SARS-CoV-2's infection and evade the immune system. Moreover, our molecular docking analysis has supported a strong protein-ligand interaction of N-acetyl-D-glucosamine with these selected proteins. Furthermore, computational analysis against the D614G mutant of the virus has shown that N-acetyl-D-glucosamine affinity and its binding potential were not affected by the mutations occurring in the virus' receptor binding domain. The analysis on the affinity of N-acetyl-D-glucosamine towards human antibodies has shown that it could potentially bind to both SARS-CoV-2 proteins and antibodies based on our predictive modelling work. Our results confirmed that N-acetyl-D-glucosamine holds the potential to inhibit several SARS-CoV-2 proteins as well as induce an immune response against the virus in the host.

Indexed as

Molecular Dynamics SimulationAcetylglucosamineAntibodies, NeutralizingAntibodies, ViralCOVID-19HumansSARS-CoV-2Viral ProteinsVirulence FactorsAcetylglucosamineAntibodies, NeutralizingAntibodies, ViralViral ProteinsVirulence Factors

Identifiers

PMID34043733
PMCPMC8158907
OpenAlexW3162767886

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.