Evidence map›Paper›PMID 32169481›Full record

ArticleThe Journal of infection2020

COVID-19 spike-host cell receptor GRP78 binding site prediction.

Ibrahim M Ibrahim, Doaa H Abdelmalek, Mohammed E Elshahat, Abdo A Elfiky

Registry-linked trialAbstract read
In one paragraph

Article in The Journal of infection, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04570254 (Open Clinical Trial of the Use of Antioxidants and Pentoxifylline as Adjuvant Therapy to Standard Therapy in Patients With and Without Septic Shock Secondary to COVID-19 Severe Pneumonia), which is not on this map. Cited by 300 papers.

0numbers the graph read from it
0cells of the map it votes in
300citing papers in PubMed
–field-weighted citation impact
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.

NCT04570254 nacompletednot on this map

Open Clinical Trial of the Use of Antioxidants and Pentoxifylline as Adjuvant Therapy to Standard Therapy in Patients With and Without Septic Shock Secondary to COVID-19 Severe Pneumonia

TypeinterventionalSponsorUnidad Temporal COVID-19 en Centro CitibanamexRan2020 to 2020Enrolled110ConditionsPneumonia, Viral, Covid19, ARDS, Oxidative StressArmsVitamin C, Vitamin E, Melatonin, N-acetyl cysteine, Pentoxifylline
3 · Its place in the literature

Who cites it

300 citing papers in PubMed.

  1. Article
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  5. Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  6. Review
  7. Stress-induced translocation of the endoplasmic reticulum chaperone GRP78/BiP and its impact on human disease and therapy.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Review
  9. Review
  10. Article
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  20. Article

240 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Ibrahim M IbrahimBiophysics Department, Faculty of Sciences, Cairo University, Giza, Egypt.
Doaa H AbdelmalekBiophysics Department, Faculty of Sciences, Cairo University, Giza, Egypt.
Mohammed E ElshahatBiophysics Department, Faculty of Sciences, Cairo University, Giza, Egypt.
Abdo A ElfikyBiophysics Department, Faculty of Sciences, Cairo University, Giza, Egypt; College of Applied Medical Sciences, University of Al-Jouf, Saudi Arabia. Electronic address: abdo@sci.cu.edu.eg.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectivesUnderstanding the novel coronavirus (COVID-19) mode of host cell recognition may help to fight the disease and save lives. The spike protein of coronaviruses is the main driving force for host cell recognition.

methodsIn this study, the COVID-19 spike binding site to the cell-surface receptor (Glucose Regulated Protein 78 (GRP78)) is predicted using combined molecular modeling docking and structural bioinformatics. The COVID-19 spike protein is modeled using its counterpart, the SARS spike.

resultsSequence and structural alignments show that four regions, in addition to its cyclic nature have sequence and physicochemical similarities to the cyclic Pep42. Protein-protein docking was performed to test the four regions of the spike that fit tightly in the GRP78 Substrate Binding Domain β (SBDβ). The docking pose revealed the involvement of the SBDβ of GRP78 and the receptor-binding domain of the coronavirus spike protein in recognition of the host cell receptor.

conclusionsWe reveal that the binding is more favorable between regions III (C391-C525) and IV (C480-C488) of the spike protein model and GRP78. Region IV is the main driving force for GRP78 binding with the predicted binding affinity of -9.8 kcal/mol. These nine residues can be used to develop therapeutics specific against COVID-19.

Indexed as

Models, MolecularBetacoronavirusBinding SitesCoronavirus InfectionsCOVID-19Endoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHumansMolecular Docking SimulationPandemicsPneumonia, ViralProtein DomainsProtein Structure, TertiarySARS-CoV-2Spike Glycoprotein, CoronavirusEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHSPA5 protein, humanSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2BiPCOVID-19 spikeGRP78Pep42Protein-protein dockingStructural bioinformatics

Identifiers

PMID32169481
PMCPMC7102553

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Registered trials

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.