Evidence map›Paper›PMID 32531235›Full record

ArticleVirus research2020

Role of the GTNGTKR motif in the N-terminal receptor-binding domain of the SARS-CoV-2 spike protein.

Nouredine Behloul, Sarra Baha, Ruihua Shi, Jihong Meng

Open access · bronzeAbstract read
In one paragraph

Article in Virus research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 12% 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

28 citing papers in PubMed, 65 citations in OpenAlex.

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  12. Structural and energetic analyses of SARS-CoV-2Computational and structural biotechnology journal · 2022
    Article
  13. Article
  14. Article
  15. Review
  16. Observational
  17. Article
  18. Recent progress on the mutations of SARS-CoV-2 spike protein and suggestions for prevention and controlling of the pandemic.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2021
    Review
  19. Article
  20. SARS-CoV-2 Proteins Bind to Hemoglobin and Its Metabolites.International journal of molecular sciences · 2021
    Article
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

4 authors at 2 institutions in 1 country.

Nouredine BehloulCollege of Basic Medicine, Shanghai University of Medicine and Health Sciences, Shanghai, 201318, China.
Sarra BahaDepartment of Gastroenterology, Zhongda Hospital, Southeast University, Nanjing, 210009, Jiangsu Province, China.
Ruihua ShiDepartment of Gastroenterology, Zhongda Hospital, Southeast University, Nanjing, 210009, Jiangsu Province, China. Electronic address: ruihuashi@126.com.
Jihong MengCollege of Basic Medicine, Shanghai University of Medicine and Health Sciences, Shanghai, 201318, China. Electronic address: jihongmeng@163.com.
Shanghai University of Medicine and Health Sciences · CNZhongda Hospital Southeast University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 2019 novel coronavirus disease (COVID-19) that emerged in China has been declared as public health emergency of international concern by the World Health Organization and the causative pathogen was named severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this report, we analyzed the structural characteristics of the N-terminal domain of the S1 subunit (S1-NTD) of the SARS-CoV-2 spike protein in comparison to the SARS-CoV in particular, and to other viruses presenting similar characteristic in general. Given the severity and the wide and rapid spread of the SARS-CoV-2 infection, it is very likely that the virus recognizes other receptors/co-receptors besides the ACE2. The NTD of the SARS-CoV-2 contains a receptor-binding motif different from that of SARS-CoV, with some insertions that could confer to the new coronavirus new receptor binding abilities. In particular, motifs similar to the insertion 72GTNGTKR78 have been found in structural proteins of other viruses; and these motifs were located in putative regions involved in recognizing protein and sugar receptors, suggesting therefore that similar binding abilities could be displayed by the SARS-CoV-2 S1-NTD. Moreover, concerning the origin of these NTD insertions, our findings point towards an evolutionary acquisition rather than the hypothesis of an engineered virus.

Indexed as

Amino Acid SequenceAngiotensin-Converting Enzyme 2AnimalsBetacoronavirusBinding SitesChiropteraCoronavirus InfectionsCOVID-19Evolution, MolecularGene ExpressionHost-Pathogen InteractionsHumansMiddle East Respiratory Syndrome CoronavirusModels, MolecularPandemicsPeptidyl-Dipeptidase AACE2 protein, humanAngiotensin-Converting Enzyme 2Peptidyl-Dipeptidase AReceptors, VirusSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2CoronavirusCOVID-19Receptor-binding domainReceptor binding-motifSARS-CoV-2

Identifiers

PMID32531235
PMCPMC7282740
OpenAlexW3033184506

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.