Evidence map›Paper›PMID 32936048›Full record

ArticleJournal of biomolecular structure & dynamics2022

Molecular basis of the potential interaction of SARS-CoV-2 spike protein to CD147 in COVID-19 associated-lymphopenia.

Mohamed A Helal, Shaimaa Shouman, Ahmad Abdelwaly, Ahmed O Elmehrath, Mohamed Essawy, Shireen M Sayed, Amr H Saleh, Nagwa El-Badri

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular structure & dynamics, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
6.2field-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

58 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
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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

8 authors at 3 institutions in 1 country.

Mohamed A HelalBiomedical Sciences Program, University of Science and Technology, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0002-6304-8285
Shaimaa ShoumanCenter of Excellence for Stem Cells and Regenerative Medicine, Zewail City of Science and Technology, Giza, Egypt.
Ahmad AbdelwalyBiomedical Sciences Program, University of Science and Technology, Zewail City of Science and Technology, Giza, Egypt.
Ahmed O ElmehrathCenter of Excellence for Stem Cells and Regenerative Medicine, Zewail City of Science and Technology, Giza, Egypt.
Mohamed EssawyCenter of Excellence for Stem Cells and Regenerative Medicine, Zewail City of Science and Technology, Giza, Egypt.
Shireen M SayedCenter of Excellence for Stem Cells and Regenerative Medicine, Zewail City of Science and Technology, Giza, Egypt.
Amr H SalehBiomedical Sciences Program, University of Science and Technology, Zewail City of Science and Technology, Giza, Egypt.ORCID 0000-0002-3175-1048
Nagwa El-BadriCenter of Excellence for Stem Cells and Regenerative Medicine, Zewail City of Science and Technology, Giza, Egypt.
Zewail City of Science and Technology · EGCairo University · EGSuez Canal University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lymphopenia is considered one of the most characteristic clinical features of the coronavirus disease 2019 (COVID-19). SARS-CoV-2 infects host cells via the interaction of its spike protein with the human angiotensin-converting enzyme 2 (hACE2) receptor. Since T lymphocytes display a very low expression level of hACE2, a novel receptor might be involved in the entry of SARS-CoV-2 into T cells. The transmembrane glycoprotein CD147 is highly expressed by activated T lymphocytes, and was recently proposed as a probable route for SARS-CoV-2 invasion. To understand the molecular basis of the potential interaction of SARS-CoV-2 to CD147, we have investigated the binding of the viral spike protein to this receptor in-silico. The results showed that this binding is dominated by electrostatic interactions involving residues Arg403, Asn481, and the backbone of Gly502. The overall binding arrangement shows the CD147 C-terminal domain interacting with the spike external subdomain in the grove between the short antiparallel β strands, β1' and β2', and the small helix α1'. This proposed interaction was further confirmed using MD simulation and binding free energy calculation. These data contribute to a better understanding of the mechanism of infection of SARS-CoV-2 to T lymphocytes and could provide valuable insights for the rational design of adjuvant treatment for COVID-19. Communicated by Ramaswamy H. Sarma.

Indexed as

COVID-19LymphopeniaBasiginHumansProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusBasiginBSG protein, humanSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2CD147dockingLymphopeniaSARS-CoV-2spike

Identifiers

PMID32936048
PMCPMC7544927
OpenAlexW3086897361

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.